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Conserved domains on  [gi|1751186567|ref|XP_030781501|]
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actin-related protein 8 isoform X2 [Rhinopithecus roxellana]

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_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
47-574 0e+00

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: 598.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  47 FIIVVHPGSTTLRIGRATDTLPASIPHVIARRHKQQGQPLYKDSW-LLREGLNKPESNEQRQNGLKMVDQAIWSKKMSNG 125
Cdd:cd10206     1 KTIVIHPGSRNLRIGRASDDLPVVIPHCIARRRKQTGSARPEDVPpAVRNGEDSVESEEEREEALKEVERALKSRKKSNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 126 TRRIP--VSPEQARSYNKQMRPAILDHCSGNKWTNTSHHPEYLVGEEALYVNPLDCYNIHWPIRRGQLNIHPgPGGSLTA 203
Cdd:cd10206    81 RRRIPnqVSAKQNKPSKPENVPEDLDASSGENWTDTSDYPDFLVGEEALRLPPSEEYNLHWPIRRGRLNVHS-DGGSLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 204 VLADIEVIWSHAIQKYLEIPLKDLKYYRCILLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVD 283
Cdd:cd10206   160 VLDDLEDIWSHALEEKLEIPRKDLKNYRAVLVIPDLFDRRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 284 VGDQKTSVCCVEDGVSHRNTRI------------FSW---------------------------------NQDISGLQDH 318
Cdd:cd10206   240 IGAQKTSVACVEDGLSIPNSRIrlpyggdditrcFLWllrrsgfpyrecnlnspldflllerlketyctlDQDDIGVQLH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 319 EFQIRHPDSPALLYQFRLgdeklqapmalfypatfgivgqkmttlqhrsqgdpedphdehyllatqskqeqsakatadrk 398
Cdd:cd10206   320 EFYVREPGQPTLKYQFKL-------------------------------------------------------------- 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 399 saskpigfegdlrgqssdlperlhsqevdlgssqgdglmagndsedaltalmsrktaislfegkaLGLDKAILHSIDCCS 478
Cdd:cd10206   338 -----------------------------------------------------------------LPLDEAIVQSILSCA 352
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 479 SDDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFrRIIENVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWI 558
Cdd:cd10206   353 SDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLF-EAVETVEVLPPPKDMDPSLLAWKGGAVLACLDSAQELWI 431
                         570
                  ....*....|....*.
gi 1751186567 559 YQREWQRFGVRMLRER 574
Cdd:cd10206   432 TRKEWQRLGVRALRER 447
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
47-574 0e+00

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: 598.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  47 FIIVVHPGSTTLRIGRATDTLPASIPHVIARRHKQQGQPLYKDSW-LLREGLNKPESNEQRQNGLKMVDQAIWSKKMSNG 125
Cdd:cd10206     1 KTIVIHPGSRNLRIGRASDDLPVVIPHCIARRRKQTGSARPEDVPpAVRNGEDSVESEEEREEALKEVERALKSRKKSNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 126 TRRIP--VSPEQARSYNKQMRPAILDHCSGNKWTNTSHHPEYLVGEEALYVNPLDCYNIHWPIRRGQLNIHPgPGGSLTA 203
Cdd:cd10206    81 RRRIPnqVSAKQNKPSKPENVPEDLDASSGENWTDTSDYPDFLVGEEALRLPPSEEYNLHWPIRRGRLNVHS-DGGSLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 204 VLADIEVIWSHAIQKYLEIPLKDLKYYRCILLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVD 283
Cdd:cd10206   160 VLDDLEDIWSHALEEKLEIPRKDLKNYRAVLVIPDLFDRRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 284 VGDQKTSVCCVEDGVSHRNTRI------------FSW---------------------------------NQDISGLQDH 318
Cdd:cd10206   240 IGAQKTSVACVEDGLSIPNSRIrlpyggdditrcFLWllrrsgfpyrecnlnspldflllerlketyctlDQDDIGVQLH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 319 EFQIRHPDSPALLYQFRLgdeklqapmalfypatfgivgqkmttlqhrsqgdpedphdehyllatqskqeqsakatadrk 398
Cdd:cd10206   320 EFYVREPGQPTLKYQFKL-------------------------------------------------------------- 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 399 saskpigfegdlrgqssdlperlhsqevdlgssqgdglmagndsedaltalmsrktaislfegkaLGLDKAILHSIDCCS 478
Cdd:cd10206   338 -----------------------------------------------------------------LPLDEAIVQSILSCA 352
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 479 SDDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFrRIIENVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWI 558
Cdd:cd10206   353 SDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLF-EAVETVEVLPPPKDMDPSLLAWKGGAVLACLDSAQELWI 431
                         570
                  ....*....|....*.
gi 1751186567 559 YQREWQRFGVRMLRER 574
Cdd:cd10206   432 TRKEWQRLGVRALRER 447
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
162-574 6.94e-25

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 106.57  E-value: 6.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  162 HPEYLVGEEAlyVNPLDCYNIHWPIRRGQL-NIHpgpggsltavlaDIEVIWSHAIQKYLEIPLKDLKyyrcILL-IPDI 239
Cdd:smart00268  44 AKDIFVGDEA--QEKRGGLELKYPIENGIVeNWD------------DMEKIWDYTFFNELRVEPEEHP----VLLtEPPM 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  240 YNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDG--VSHRNTRIFSWNQDISG-LQ 316
Cdd:smart00268 106 NPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGyvLPHAIKRIDIAGRDITDyLK 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  317 DH-EFQIRHPDSPALLYQFRLGDEKLqAPMALFYPatfgivgQKMTtlqhrsqgdpedphdehyllatqsKQEQSAKATA 395
Cdd:smart00268 186 ELlSERGYQFNSSAEFEIVREIKEKL-CYVAEDFE-------KEMK------------------------LARESSESSK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  396 DRKSASKPIGFEGDLRGQSSDLPERLHSQEvdlgssqgdglMAGNDSEdaltalmsrktaislfegkalGLDKAILHSID 475
Cdd:smart00268 234 LEKTYELPDGNTIKVGNERFRIPEILFSPE-----------LIGLEQK---------------------GIHELVYESIQ 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  476 CCSSdDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriienVDVITRPkdmDPRLIAWKGGAVLACLDTTQE 555
Cdd:smart00268 282 KCDI-DVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPKKLK-----VKVIAPP---ERKYSVWLGGSILASLSTFED 352
                          410
                   ....*....|....*....
gi 1751186567  556 LWIYQREWQRFGVRMLRER 574
Cdd:smart00268 353 MWITKKEYEESGSQIVERK 371
Actin pfam00022
Actin;
141-569 4.34e-18

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 86.59  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 141 KQMRPAILDHCSGNKWTNTShhpEYLVGEEALYVNPldCYNIHWPIRRGqlnihpgpggsltaVLADIEV---IWSHAIQ 217
Cdd:pfam00022  24 KAVIPSCVGKPRGTKVEAAN---KYYVGDEALTYRP--GMEVRSPVEDG--------------IVVDWDAmeeIWEHVLK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 218 KYLEIPLKDlkyyRCILLIPDIYNKQHVKELVNMILM-KMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVED 296
Cdd:pfam00022  85 EELQVDPEE----HPLLLTEPPWNPPANREKAAEIMFeKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 297 G-VSHRNTRifswNQDISG--LQDhefQIRHpdspallyQFRLGDEKLqAPMALFYPATFGIVGQKMTTLQHRSQGDPED 373
Cdd:pfam00022 161 GyVLQKAIR----RSDLGGdfLTD---YLRE--------LLRSRNIEI-TPRYLIKSKKPGDPAPAVTKRELPDTTYSYK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 374 PHDEHYLLatqskqeQSAKATADRKSaskpIGFEGDLRgQSSDLPERLH----SQEVDLGSSQ---GDGL----MAGNDS 442
Cdd:pfam00022 225 TYQERRVL-------EEIKESVCYVS----DDPFGDET-TSSSIPTRVYelpdGSTIILGAERfrvPEILfnpsLIGSES 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 443 EDAltalmsrktaislFEGKALGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRrii 522
Cdd:pfam00022 293 ELP-------------PPQTAVGIPELIVDAINACDVD-LRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVK--- 355
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1751186567 523 enVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWIYQREWQRFGVR 569
Cdd:pfam00022 356 --VKIIAPGNTVERRYSAWIGGSILASLGTFQQMWVSKQEYEEHGAS 400
PTZ00466 PTZ00466
actin-like protein; Provisional
464-575 1.66e-07

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 53.79  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 464 LGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEflqhRILNKMppsfRRIIenvdvitrPKDMDPRLIA--- 540
Cdd:PTZ00466  277 LGLSELIVTSITRADMD-LRRTLYSHIVLSGGTTMFHGFGD----RLLNEI----RKFA--------PKDITIRISAppe 339
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1751186567 541 -----WKGGAVLACLDTTQELWIYQREWQRFGVRMLRERA 575
Cdd:PTZ00466  340 rkfstFIGGSILASLATFKKIWISKQEFDEYGSVILHRKT 379
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
47-574 0e+00

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: 598.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  47 FIIVVHPGSTTLRIGRATDTLPASIPHVIARRHKQQGQPLYKDSW-LLREGLNKPESNEQRQNGLKMVDQAIWSKKMSNG 125
Cdd:cd10206     1 KTIVIHPGSRNLRIGRASDDLPVVIPHCIARRRKQTGSARPEDVPpAVRNGEDSVESEEEREEALKEVERALKSRKKSNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 126 TRRIP--VSPEQARSYNKQMRPAILDHCSGNKWTNTSHHPEYLVGEEALYVNPLDCYNIHWPIRRGQLNIHPgPGGSLTA 203
Cdd:cd10206    81 RRRIPnqVSAKQNKPSKPENVPEDLDASSGENWTDTSDYPDFLVGEEALRLPPSEEYNLHWPIRRGRLNVHS-DGGSLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 204 VLADIEVIWSHAIQKYLEIPLKDLKYYRCILLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVD 283
Cdd:cd10206   160 VLDDLEDIWSHALEEKLEIPRKDLKNYRAVLVIPDLFDRRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 284 VGDQKTSVCCVEDGVSHRNTRI------------FSW---------------------------------NQDISGLQDH 318
Cdd:cd10206   240 IGAQKTSVACVEDGLSIPNSRIrlpyggdditrcFLWllrrsgfpyrecnlnspldflllerlketyctlDQDDIGVQLH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 319 EFQIRHPDSPALLYQFRLgdeklqapmalfypatfgivgqkmttlqhrsqgdpedphdehyllatqskqeqsakatadrk 398
Cdd:cd10206   320 EFYVREPGQPTLKYQFKL-------------------------------------------------------------- 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 399 saskpigfegdlrgqssdlperlhsqevdlgssqgdglmagndsedaltalmsrktaislfegkaLGLDKAILHSIDCCS 478
Cdd:cd10206   338 -----------------------------------------------------------------LPLDEAIVQSILSCA 352
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 479 SDDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFrRIIENVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWI 558
Cdd:cd10206   353 SDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLF-EAVETVEVLPPPKDMDPSLLAWKGGAVLACLDSAQELWI 431
                         570
                  ....*....|....*.
gi 1751186567 559 YQREWQRFGVRMLRER 574
Cdd:cd10206   432 TRKEWQRLGVRALRER 447
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
207-567 8.98e-29

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: 114.90  E-value: 8.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 207 DIEVIWSHAIQKYLEIPLKDlkyYRCILLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGD 286
Cdd:cd10169    28 DMEKIWEHVFYNLLRVDPEE---HPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 287 QKTSVCCVEDGVSHRNTrifswnqdisglqdhefqIRHPDspallyqfrlgdeklqapmalfypatFGivGQKMTT-LQH 365
Cdd:cd10169   105 GVTHIVPVYEGYVLPHA------------------VRRLD--------------------------IG--GRDLTDyLAK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 366 --RSQGDPEDPHDEHYLLatqskqeqsakatadrksaskpigfegdlrgqsSDLPERLhsqevdlgssqgdglmagndse 443
Cdd:cd10169   139 llREKGYSFSTSAEREIV---------------------------------RDIKEKL---------------------- 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 444 daltalmsrktaislfegkaLGLDKAILHSIDCCSsDDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriie 523
Cdd:cd10169   164 --------------------CGLHELIYDSIMKCD-IDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVK---- 218
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1751186567 524 nVDVITRPkdmDPRLIAWKGGAVLACLDTTQELWIYQREWQRFG 567
Cdd:cd10169   219 -VKVIAPP---ERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
162-574 6.94e-25

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 106.57  E-value: 6.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  162 HPEYLVGEEAlyVNPLDCYNIHWPIRRGQL-NIHpgpggsltavlaDIEVIWSHAIQKYLEIPLKDLKyyrcILL-IPDI 239
Cdd:smart00268  44 AKDIFVGDEA--QEKRGGLELKYPIENGIVeNWD------------DMEKIWDYTFFNELRVEPEEHP----VLLtEPPM 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  240 YNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDG--VSHRNTRIFSWNQDISG-LQ 316
Cdd:smart00268 106 NPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGyvLPHAIKRIDIAGRDITDyLK 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  317 DH-EFQIRHPDSPALLYQFRLGDEKLqAPMALFYPatfgivgQKMTtlqhrsqgdpedphdehyllatqsKQEQSAKATA 395
Cdd:smart00268 186 ELlSERGYQFNSSAEFEIVREIKEKL-CYVAEDFE-------KEMK------------------------LARESSESSK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  396 DRKSASKPIGFEGDLRGQSSDLPERLHSQEvdlgssqgdglMAGNDSEdaltalmsrktaislfegkalGLDKAILHSID 475
Cdd:smart00268 234 LEKTYELPDGNTIKVGNERFRIPEILFSPE-----------LIGLEQK---------------------GIHELVYESIQ 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567  476 CCSSdDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriienVDVITRPkdmDPRLIAWKGGAVLACLDTTQE 555
Cdd:smart00268 282 KCDI-DVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPKKLK-----VKVIAPP---ERKYSVWLGGSILASLSTFED 352
                          410
                   ....*....|....*....
gi 1751186567  556 LWIYQREWQRFGVRMLRER 574
Cdd:smart00268 353 MWITKKEYEESGSQIVERK 371
Actin pfam00022
Actin;
141-569 4.34e-18

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 86.59  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 141 KQMRPAILDHCSGNKWTNTShhpEYLVGEEALYVNPldCYNIHWPIRRGqlnihpgpggsltaVLADIEV---IWSHAIQ 217
Cdd:pfam00022  24 KAVIPSCVGKPRGTKVEAAN---KYYVGDEALTYRP--GMEVRSPVEDG--------------IVVDWDAmeeIWEHVLK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 218 KYLEIPLKDlkyyRCILLIPDIYNKQHVKELVNMILM-KMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVED 296
Cdd:pfam00022  85 EELQVDPEE----HPLLLTEPPWNPPANREKAAEIMFeKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 297 G-VSHRNTRifswNQDISG--LQDhefQIRHpdspallyQFRLGDEKLqAPMALFYPATFGIVGQKMTTLQHRSQGDPED 373
Cdd:pfam00022 161 GyVLQKAIR----RSDLGGdfLTD---YLRE--------LLRSRNIEI-TPRYLIKSKKPGDPAPAVTKRELPDTTYSYK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 374 PHDEHYLLatqskqeQSAKATADRKSaskpIGFEGDLRgQSSDLPERLH----SQEVDLGSSQ---GDGL----MAGNDS 442
Cdd:pfam00022 225 TYQERRVL-------EEIKESVCYVS----DDPFGDET-TSSSIPTRVYelpdGSTIILGAERfrvPEILfnpsLIGSES 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 443 EDAltalmsrktaislFEGKALGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRrii 522
Cdd:pfam00022 293 ELP-------------PPQTAVGIPELIVDAINACDVD-LRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVK--- 355
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1751186567 523 enVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWIYQREWQRFGVR 569
Cdd:pfam00022 356 --VKIIAPGNTVERRYSAWIGGSILASLGTFQQMWVSKQEYEEHGAS 400
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
457-567 4.68e-12

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: 67.60  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 457 SLFEGKALGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSfrriiENVDVITRPkdmDP 536
Cdd:cd13397   258 SLIGREAPGIHKLVYNSIMKCDID-IRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSS-----TKVKVIAPP---ER 328
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1751186567 537 RLIAWKGGAVLACLDTTQELWIYQREWQRFG 567
Cdd:cd13397   329 KYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
163-563 3.89e-11

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: 65.28  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 163 PEYLVGEEALYVnPLDCYNIHWPIRRGqlnihpgpggsltaVLAD---IEVIWSHAIQKYL-----EIPlkdlkyyrcIL 234
Cdd:cd13395    55 RKYYIGTNSIGV-PRPNMEVISPLKDG--------------LIEDwdaFEKLWDHALKNRLrvdpsEHP---------LL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 235 LIPDIYNKQHVKE-LVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDG-VSHRNTRifswNQDI 312
Cdd:cd13395   111 LTEPSWNTRANREkLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGATSTSVVPVHDGyVLQKAIV----RSPL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 313 SG----------LQDHEFQIRHPdspallYQFRlgdeKLQAPMALFYPATFGIVGQKMTTLQHRSQGDP--EDPHDEHYL 380
Cdd:cd13395   187 GGdfltdqllklLESKNIEIIPR------YMIK----SKEPVEGGAPAKYTKKDLPNTTSSYHRYMVRRvlQDFKESVCQ 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 381 LATQSKQEQSAKATAdrksaskPIGFEgdlrgqssdLPerlHSQEVDLGSSQ---GDGLMAGNDSEDaltalmsrKTAIS 457
Cdd:cd13395   257 VSDSPFDESEAASIP-------TVSYE---------LP---DGYNIEFGAERfkiPELLFDPSLVKG--------IPAPP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 458 LFEGKALGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriienVDVITRPKDMDPR 537
Cdd:cd13395   310 SEGNELLGLPQLVYTSIGSCDVD-IRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLK-----LKILASGNTVERR 383
                         410       420
                  ....*....|....*....|....*.
gi 1751186567 538 LIAWKGGAVLACLDTTQELWIYQREW 563
Cdd:cd13395   384 FSSWIGGSILASLGSFQQMWISKQEY 409
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
457-567 2.35e-09

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: 59.36  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 457 SLFEGKALGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQhRILNKMPPSfrriiENVDVITRPkdmDP 536
Cdd:cd10214   260 SLIGSKQPGLHTLTMNSLNKCDAN-LKKDLAKNILLCGGSTMFDGFPDRFQ-KELSKLCPN-----DNPIVAASP---ER 329
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1751186567 537 RLIAWKGGAVLACLDTTQELWIYQREWQRFG 567
Cdd:cd10214   330 KYSVWTGGSILASLKSFQQLWVRRREYEERG 360
PTZ00466 PTZ00466
actin-like protein; Provisional
464-575 1.66e-07

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 53.79  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 464 LGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEflqhRILNKMppsfRRIIenvdvitrPKDMDPRLIA--- 540
Cdd:PTZ00466  277 LGLSELIVTSITRADMD-LRRTLYSHIVLSGGTTMFHGFGD----RLLNEI----RKFA--------PKDITIRISAppe 339
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1751186567 541 -----WKGGAVLACLDTTQELWIYQREWQRFGVRMLRERA 575
Cdd:PTZ00466  340 rkfstFIGGSILASLATFKKIWISKQEFDEYGSVILHRKT 379
PTZ00452 PTZ00452
actin; Provisional
145-574 2.16e-07

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 53.22  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 145 PAILDHCSGNKWTNTSHHPEYLVGEEAlyvnpldcynihwPIRRGQLNIHPGPGGSLTAVLADIEVIWSHAIQKYLEIPL 224
Cdd:PTZ00452   32 PAIVGRSKQNDGIFSTFNKEYYVGEEA-------------QAKRGVLAIKEPIQNGIINSWDDIEIIWHHAFYNELCMSP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 225 KDLKYYRCILLIPDIYNKQHVKELvnmILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDG--VSHRN 302
Cdd:PTZ00452   99 EDQPVFMTDAPMNSKFNRERMTQI---MFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVFEGhqIPQAI 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 303 TRIfswnqDISG--LQDHEFQIRHpdspallyqfRLGdeklqapMALFYPATFGIVgqkmTTLQHRSQGDPEDPHDEHYL 380
Cdd:PTZ00452  176 TKI-----NLAGrlCTDYLTQILQ----------ELG-------YSLTEPHQRIIV----KNIKERLCYTALDPQDEKRI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 381 LATQSKQEQSAKatadrksaskpigfegdlrgqssdLPErlhsqevdlgssqgdglmaGNdsedaLTALMSRKTAIS--L 458
Cdd:PTZ00452  230 YKESNSQDSPYK------------------------LPD-------------------GN-----ILTIKSQKFRCSeiL 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 459 FEGKALGLDKAILH-----SIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriienVDVITRPkd 533
Cdd:PTZ00452  262 FQPKLIGLEVAGIHhlaysSIKKCDLD-LRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLK-----IQVAAPP-- 333
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1751186567 534 mDPRLIAWKGGAVLACLDTTQELWIYQREWQRFGVRMLRER 574
Cdd:PTZ00452  334 -DRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRK 373
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
179-298 3.25e-07

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: 52.69  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 179 CYNIHWPIRRGQlnihpgpggslTAVLADIEVIWSHAIQKYLEIPLKDLKYYrcILLIPDIYNKQHVKELVNMILM-KMG 257
Cdd:cd10208    32 RVEIIWPIQDGR-----------VVDWDALEALWRHILFSLLSIPRPTNNSP--VLLSVPPSWSKSDLELLTQLFFeRLN 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1751186567 258 FSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDGV 298
Cdd:cd10208    99 VPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQ 139
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
458-567 3.77e-07

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: 52.37  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 458 LFEGKALGLDKAILH-----SIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriienVDVITRPk 532
Cdd:cd10224   256 LFQPSFLGMEAAGIHettynSIMKCDVD-IRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK-----IKIVAPP- 328
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1751186567 533 dmDPRLIAWKGGAVLACLDTTQELWIYQREWQRFG 567
Cdd:cd10224   329 --ERKYSVWIGGSILASLSTFQQMWISKQEYDESG 361
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
463-575 6.07e-07

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: 51.78  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 463 ALGLDKAILHSIdcCSSD-DTKKKMYSSILVVGGGLMFhkaQEFLQhRILNKMppsfRRIIenvdvitrPKDMDPRLIA- 540
Cdd:cd10216   267 YPGVHEVLVDSI--QKSDlDLRKTLYSNIVLSGGSTLF---KGFGD-RLLSEV----KKLA--------PKDVKIRISAp 328
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1751186567 541 -------WKGGAVLACLDTTQELWIYQREWQRFGVRMLRERA 575
Cdd:cd10216   329 perlystWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
PTZ00004 PTZ00004
actin-2; Provisional
463-567 7.70e-07

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 51.69  E-value: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 463 ALGLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriienVDVITRPKDMDPrliAWK 542
Cdd:PTZ00004  274 PPGIHELTFQSINKCDID-IRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPSTMK-----IKVVAPPERKYS---VWI 344
                          90       100
                  ....*....|....*....|....*
gi 1751186567 543 GGAVLACLDTTQELWIYQREWQRFG 567
Cdd:PTZ00004  345 GGSILSSLPTFQQMWVTKEEYDESG 369
PTZ00281 PTZ00281
actin; Provisional
457-574 1.38e-06

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 50.85  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 457 SLFEGKALGLDKAILH-----SIDCCSSDdTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRriienVDVITRP 531
Cdd:PTZ00281  261 ALFQPSFLGMESAGIHettynSIMKCDVD-IRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMK-----IKIIAPP 334
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1751186567 532 kdmDPRLIAWKGGAVLACLDTTQELWIYQREWQRFGVRMLRER 574
Cdd:PTZ00281  335 ---ERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRK 374
Actin_micro pfam17003
Putative actin-like family; This is a family of microsporidial-specific proteins of unknown ...
218-300 1.08e-05

Putative actin-like family; This is a family of microsporidial-specific proteins of unknown function. There is distant homology to the Actin family.


Pssm-ID: 374929  Cd Length: 350  Bit Score: 47.83  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 218 KYLEIPLKDLkyYRCiLLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDG 297
Cdd:pfam17003  90 GKENINPKDS--FVS-LVFHDTLNRSEILNLVDLFLNISGFKGILLLPYSLSMCIGLGIQSCIVISEYEKHTTVSLVEDY 166

                  ...
gi 1751186567 298 VSH 300
Cdd:pfam17003 167 VLF 169
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
465-567 2.97e-05

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: 46.39  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 465 GLDKAILHSIDCCSSDdTKKKMYSSILVVGGGLMFhkaqeflqhrilnkmpPSFRRIIEN---------VDV-ITRPkdM 534
Cdd:cd10210   296 GIAEAIVQSINACPEE-LQPLLYANIVLTGGNALF----------------PGFRERLEAelrslapddYDVnVTLP--E 356
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1751186567 535 DPRLIAWKGGAVLACLDTTQELWIYQREWQRFG 567
Cdd:cd10210   357 DPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
248-548 3.60e-05

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: 46.23  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 248 LVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDGvshrntrifswnqdisglqdhefQIRHPDS 327
Cdd:cd10209   100 LTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVWEG-----------------------AIQHNAV 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 328 pallyqfrlgdeklqapmalfypATFGIVGQKMTTLQHRSQGDpEDPHDEHYLLATQSKQEQSAKATADRKSASKPIGFE 407
Cdd:cd10209   157 -----------------------RRFEIGGRDLTELLAAELGK-SNPKVKLDRSIVERLKEAVAWSADDEEAYEKKVLTC 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 408 GDLRGQssdLPErlhsqevdlgssqGDGLMAGNDSEDALTALMSRktaiSLFEGKALGLDKAILHSIDCCSSdDTKKKMY 487
Cdd:cd10209   213 SPETYT---LPD-------------GRVISVGKERYCVGEALFRP----SILGIEEYGIVEQLVRAVSTSPS-ENRRQLL 271
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751186567 488 SSILVVGGGLMFHKAQEFLQHRILNKMPPSFRRIienvdVITRPKDMDPRLI---AWKGGAVLA 548
Cdd:cd10209   272 ENIVLCGGTSSVPGLEARLQKEIRLLSSPSSRPA-----LVKPPEYMPENTLrysAWIGGAILA 330
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
207-314 2.77e-04

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: 43.32  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 207 DIEVIWSHAIQKYLEIPLKDLKyyrcILLI-PDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVG 285
Cdd:cd10220    78 DMEHLWDYTFGEKLKIDPRECK----ILLTePPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSG 153
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1751186567 286 DQKTSVCCVEDGVS--HRNTRIfswnqDISG 314
Cdd:cd10220   154 DGVTHIVPVYEGFSlpHLTRRL-----DVAG 179
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
164-292 6.40e-04

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: 42.20  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 164 EYLVGEEALYvNPLDCyNIHWPIRRGqlNIHPGPGGSLTAVladiEVIWSHAIQKyLEIPLKDLKYyrCILLIP---DIY 240
Cdd:cd24009    44 EVLFGDEALE-NRLAL-DLRRPLEDG--VIKEGDDRDLEAA----RELLQHLIEL-ALPGPDDEIY--AVIGVParaSAE 112
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1751186567 241 NKQHVKELVNMIlmkmgFSGIVVHQESVCATYGSG-LSSTCIVDVGDQKTSVC 292
Cdd:cd24009   113 NKQALLEIAREL-----VDGVMVVSEPFAVAYGLDrLDNSLIVDIGAGTTDLC 160
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
465-573 8.91e-04

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: 41.79  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751186567 465 GLDKAILHSIdCCSSDDTKKKMYSSILVVGGGLMFhkaqEFLQHRILNkmppSFRRIIENVDVITRPKDMDPRLIAWKGG 544
Cdd:cd10211   245 GLVETIEFVL-KRYPAEQQDRLVQNVFLTGGNALF----PGLKERLEK----ELRAIRPFGSPFNVVRAKDPVLDAWRGA 315
                          90       100
                  ....*....|....*....|....*....
gi 1751186567 545 AVLACLDTTQELWIYQREWQRFGVRMLRE 573
Cdd:cd10211   316 AKWALDSTFEKVWITKQEYEEKGGEYLKE 344
Actin_micro pfam17003
Putative actin-like family; This is a family of microsporidial-specific proteins of unknown ...
540-577 1.88e-03

Putative actin-like family; This is a family of microsporidial-specific proteins of unknown function. There is distant homology to the Actin family.


Pssm-ID: 374929  Cd Length: 350  Bit Score: 40.90  E-value: 1.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1751186567 540 AWKGGAVLACLDTTQELWIYQREWQRFGVRMLRERAAF 577
Cdd:pfam17003 311 ILRGAKVFNNLELSKELWLTDKEWNSVRLRVLKEKVLF 348
 
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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