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Conserved domains on  [gi|1028571264|gb|OAJ39568|]
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hypothetical protein BDEG_23403 [Batrachochytrium dendrobatidis JEL423]

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_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
137-459 1.28e-144

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: 417.48  E-value: 1.28e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 137 WVQPIQNGQVADWDALQVLWRKILVNHCGVERATNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYG 216
Cdd:cd10208    35 IIWPIQDGRVVDWDALEALWRHILFSLLSIPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 217 AGVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSGDEKFV---ASYGKYIGKDLARAFIQSPAF 293
Cdd:cd10208   115 AGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELksqAESGEEATLDLAEALKKSPIC 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 294 FAPSLSGIeqpnaefDFKGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHLVVSNSCEPEKRLFLWENILLVGGCSL 373
Cdd:cd10208   195 EVLSDGAD-------LASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASDEPDKRPALWENIIIVGGGSR 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 374 IRGIKDRIESEL-AVLLAASETSSEYQAKDVKWIKLPDYFVEFKDRS-CDAAFLGGSITAKLVFT-SSGAMYLTRADYDE 450
Cdd:cd10208   268 IRGLKEALLSELqQFHLISETSASPQQPRIIRLAKIPDYFPEWKKSGyEEAAFLGASIVAKLVFNdPSSKHYISKVDYNE 347

                  ....*....
gi 1028571264 451 FGPAASFLK 459
Cdd:cd10208   348 KGPAAIHTK 356
 
Name Accession Description Interval E-value
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
137-459 1.28e-144

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: 417.48  E-value: 1.28e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 137 WVQPIQNGQVADWDALQVLWRKILVNHCGVERATNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYG 216
Cdd:cd10208    35 IIWPIQDGRVVDWDALEALWRHILFSLLSIPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 217 AGVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSGDEKFV---ASYGKYIGKDLARAFIQSPAF 293
Cdd:cd10208   115 AGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELksqAESGEEATLDLAEALKKSPIC 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 294 FAPSLSGIeqpnaefDFKGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHLVVSNSCEPEKRLFLWENILLVGGCSL 373
Cdd:cd10208   195 EVLSDGAD-------LASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASDEPDKRPALWENIIIVGGGSR 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 374 IRGIKDRIESEL-AVLLAASETSSEYQAKDVKWIKLPDYFVEFKDRS-CDAAFLGGSITAKLVFT-SSGAMYLTRADYDE 450
Cdd:cd10208   268 IRGLKEALLSELqQFHLISETSASPQQPRIIRLAKIPDYFPEWKKSGyEEAAFLGASIVAKLVFNdPSSKHYISKVDYNE 347

                  ....*....
gi 1028571264 451 FGPAASFLK 459
Cdd:cd10208   348 KGPAAIHTK 356
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
140-455 1.21e-58

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 197.10  E-value: 1.21e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  140 PIQNGQVADWDALQVLWRKILVNHCGVEraTNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGV 219
Cdd:smart00268  65 PIENGIVENWDDMEKIWDYTFFNELRVE--PEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGR 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  220 TSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMS--------GDEKFVASYGK----YIGKDLARAF 287
Cdd:smart00268 143 TTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSergyqfnsSAEFEIVREIKeklcYVAEDFEKEM 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  288 IQSPAFFAPSLSGIEQPNAEfdfkGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHLVVsNSCEPEKRLFLWENILL 367
Cdd:smart00268 223 KLARESSESSKLEKTYELPD----GNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESI-QKCDIDVRKDLYENIVL 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  368 VGGCSLIRGIKDRIESELAVLLAASETsseyqakdVKWIKLPdyfvefkDRSCdAAFLGGSITAKLvfTSSGAMYLTRAD 447
Cdd:smart00268 298 SGGSTLIPGFGERLEKELKQLAPKKLK--------VKVIAPP-------ERKY-SVWLGGSILASL--STFEDMWITKKE 359

                   ....*...
gi 1028571264  448 YDEFGPAA 455
Cdd:smart00268 360 YEESGSQI 367
Actin pfam00022
Actin;
140-453 1.65e-49

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 174.03  E-value: 1.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 140 PIQNGQVADWDALQVLWRKILVNHCGVERATNinPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGV 219
Cdd:pfam00022  63 PVEDGIVVDWDAMEEIWEHVLKEELQVDPEEH--PLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGR 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 220 TSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSG---------------------------DEKFV 272
Cdd:pfam00022 141 TTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSrnieitprylikskkpgdpapavtkreLPDTT 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 273 ASYGKYIGKDLARAFIQ-----SPAFFAPSLSGIEQPNAEFDF-KGQKIDIGSWGFRAIDVLFKPELIG--------KDV 338
Cdd:pfam00022 221 YSYKTYQERRVLEEIKEsvcyvSDDPFGDETTSSSIPTRVYELpDGSTIILGAERFRVPEILFNPSLIGseselpppQTA 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 339 PGIHDAMHLVVsNSCEPEKRLFLWENILLVGGCSLIRGIKDRIESELAVLlaaseTSSEYQAKdvkwIKLPDYFVEFKdr 418
Cdd:pfam00022 301 VGIPELIVDAI-NACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQL-----APPGVKVK----IIAPGNTVERR-- 368
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1028571264 419 scDAAFLGGSITAKL-VFtssGAMYLTRADYDEFGP 453
Cdd:pfam00022 369 --YSAWIGGSILASLgTF---QQMWVSKQEYEEHGA 399
PTZ00004 PTZ00004
actin-2; Provisional
86-455 3.16e-49

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 172.26  E-value: 3.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  86 MMVDSPSHAVVANTATTTVSPAAVADELRVN-----TRHDANESGKGSAS------DHASS-----AWVQPIQNGQVADW 149
Cdd:PTZ00004    1 MSVEETNAAVVDNGSGMVKAGFAGDDAPRCVfpsivGRPKNPGIMVGMEEkdcyvgDEAQDkrgilTLKYPIEHGIVTNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 150 DALQVLWRKILVNHcgVERATNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLVVDIGH 229
Cdd:PTZ00004   81 DDMEKIWHHTFYNE--LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 230 TTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSG--------DEKFVASYGK----YIGKDLArafiqspAFFAPS 297
Cdd:PTZ00004  159 GVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHErgttftttAEKEIVRDIKeklcYIALDFD-------EEMGNS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 298 LSGIEQPNAEFDF-KGQKIDIGSWGFRAIDVLFKPELIGKDVP-GIHDamhLVVS--NSCEPEKRLFLWENILLVGGCSL 373
Cdd:PTZ00004  232 AGSSDKYEESYELpDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHE---LTFQsiNKCDIDIRKDLYGNIVLSGGTTM 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 374 IRGIKDRIESELAVLLAASETSSEYQAKDVKwiklpdyfvefkdrscDAAFLGGSITAKLvfTSSGAMYLTRADYDEFGP 453
Cdd:PTZ00004  309 YRGLPERLTKELTTLAPSTMKIKVVAPPERK----------------YSVWIGGSILSSL--PTFQQMWVTKEEYDESGP 370

                  ..
gi 1028571264 454 AA 455
Cdd:PTZ00004  371 SI 372
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
205-390 3.11e-05

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: 45.84  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 205 FLLDQPVAALYGAGV----TSG-LVVDIGHTTTDIspvfenvAVYS-----ASVTIAVGGQNIETYLVQLMSgdEKfvas 274
Cdd:COG1077   131 YLIEEPMAAAIGAGLpieePTGnMVVDIGGGTTEV-------AVISlggivVSRSIRVAGDELDEAIIQYVR--KK---- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 275 YGKYIG--------KDLARAFiqspaffapslsgIEQPNAEFDFKGQ--------KIDIGSwgfraIDVLfkpELIGKDV 338
Cdd:COG1077   198 YNLLIGertaeeikIEIGSAY-------------PLEEELTMEVRGRdlvtglpkTITITS-----EEIR---EALEEPL 256
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1028571264 339 PGIHDAMHLVVSNsCEPEKRLFLWEN-ILLVGGCSLIRGIKDRIESE--LAVLLA 390
Cdd:COG1077   257 NAIVEAIKSVLEK-TPPELAADIVDRgIVLTGGGALLRGLDKLLSEEtgLPVHVA 310
 
Name Accession Description Interval E-value
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
137-459 1.28e-144

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: 417.48  E-value: 1.28e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 137 WVQPIQNGQVADWDALQVLWRKILVNHCGVERATNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYG 216
Cdd:cd10208    35 IIWPIQDGRVVDWDALEALWRHILFSLLSIPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 217 AGVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSGDEKFV---ASYGKYIGKDLARAFIQSPAF 293
Cdd:cd10208   115 AGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELksqAESGEEATLDLAEALKKSPIC 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 294 FAPSLSGIeqpnaefDFKGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHLVVSNSCEPEKRLFLWENILLVGGCSL 373
Cdd:cd10208   195 EVLSDGAD-------LASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASDEPDKRPALWENIIIVGGGSR 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 374 IRGIKDRIESEL-AVLLAASETSSEYQAKDVKWIKLPDYFVEFKDRS-CDAAFLGGSITAKLVFT-SSGAMYLTRADYDE 450
Cdd:cd10208   268 IRGLKEALLSELqQFHLISETSASPQQPRIIRLAKIPDYFPEWKKSGyEEAAFLGASIVAKLVFNdPSSKHYISKVDYNE 347

                  ....*....
gi 1028571264 451 FGPAASFLK 459
Cdd:cd10208   348 KGPAAIHTK 356
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
140-455 1.21e-58

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 197.10  E-value: 1.21e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  140 PIQNGQVADWDALQVLWRKILVNHCGVEraTNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGV 219
Cdd:smart00268  65 PIENGIVENWDDMEKIWDYTFFNELRVE--PEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGR 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  220 TSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMS--------GDEKFVASYGK----YIGKDLARAF 287
Cdd:smart00268 143 TTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSergyqfnsSAEFEIVREIKeklcYVAEDFEKEM 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  288 IQSPAFFAPSLSGIEQPNAEfdfkGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHLVVsNSCEPEKRLFLWENILL 367
Cdd:smart00268 223 KLARESSESSKLEKTYELPD----GNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESI-QKCDIDVRKDLYENIVL 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  368 VGGCSLIRGIKDRIESELAVLLAASETsseyqakdVKWIKLPdyfvefkDRSCdAAFLGGSITAKLvfTSSGAMYLTRAD 447
Cdd:smart00268 298 SGGSTLIPGFGERLEKELKQLAPKKLK--------VKVIAPP-------ERKY-SVWLGGSILASL--STFEDMWITKKE 359

                   ....*...
gi 1028571264  448 YDEFGPAA 455
Cdd:smart00268 360 YEESGSQI 367
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
88-455 7.68e-56

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: 189.14  E-value: 7.68e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  88 VDSPSHAVVANTATTTVSPAAVadelrVNTRHDANESGKGSASDHASSAWVQPIQNGQVADWDALQVLWRKILVNHCGVE 167
Cdd:cd10209     3 IDAGSRLLKAGYAYPDREPSVV-----EPTRVTPAVEDGEESDTVVEGNTVSPIRRGRIEDWDALEALLRYVFYTGLGWE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 168 RAtNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLVVDIGHTTTDISPVFENVAVYSAS 247
Cdd:cd10209    78 EG-NEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVWEGAIQHNAV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 248 VTIAVGGQNIETYLVQLMSGDEKFVasygKYIGKDLARAFIQ-------SPAFFAPSLSGIEQPNAEFDfkGQKIDIGSW 320
Cdd:cd10209   157 RRFEIGGRDLTELLAAELGKSNPKV----KLDRSIVERLKEAvawsaddEEAYEKKVLTCSPETYTLPD--GRVISVGKE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 321 GFRAIDVLFKPELIGKDVPGIHDAMHLVVSnSCEPEKRLFLWENILLVGGCSLIRGIKDRIESELAVLLAASETSSeyqa 400
Cdd:cd10209   231 RYCVGEALFRPSILGIEEYGIVEQLVRAVS-TSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSRPA---- 305
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1028571264 401 kdvkWIKLPDYFVEFKDRScdAAFLGGSITAKLVFTSSGamYLTRADYDEFGPAA 455
Cdd:cd10209   306 ----LVKPPEYMPENTLRY--SAWIGGAILAKVVFPQNQ--HVTKADYDETGPSV 352
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
149-452 2.69e-54

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: 181.92  E-value: 2.69e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 149 WDALQVLWRKILVNHCGVEraTNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLVVDIG 228
Cdd:cd10169    26 WDDMEKIWEHVFYNLLRVD--PEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 229 HTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSGDEKFVASygkYIGKDLARafiqspaffapslsgieqpnaef 308
Cdd:cd10169   104 EGVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFST---SAEREIVR----------------------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 309 DFKgqkidigswgfraidvlfkpeligKDVPGIHDAMHLVVsNSCEPEKRLFLWENILLVGGCSLIRGIKDRIESELAVL 388
Cdd:cd10169   158 DIK------------------------EKLCGLHELIYDSI-MKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKL 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028571264 389 LAASETsseyqakdVKWIKLPdyfvefkDRSCdAAFLGGSITAKLvfTSSGAMYLTRADYDEFG 452
Cdd:cd10169   213 APSSVK--------VKVIAPP-------ERKY-SAWIGGSILASL--STFQQMWITKEEYEEHG 258
Actin pfam00022
Actin;
140-453 1.65e-49

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 174.03  E-value: 1.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 140 PIQNGQVADWDALQVLWRKILVNHCGVERATNinPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGV 219
Cdd:pfam00022  63 PVEDGIVVDWDAMEEIWEHVLKEELQVDPEEH--PLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGR 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 220 TSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSG---------------------------DEKFV 272
Cdd:pfam00022 141 TTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSrnieitprylikskkpgdpapavtkreLPDTT 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 273 ASYGKYIGKDLARAFIQ-----SPAFFAPSLSGIEQPNAEFDF-KGQKIDIGSWGFRAIDVLFKPELIG--------KDV 338
Cdd:pfam00022 221 YSYKTYQERRVLEEIKEsvcyvSDDPFGDETTSSSIPTRVYELpDGSTIILGAERFRVPEILFNPSLIGseselpppQTA 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 339 PGIHDAMHLVVsNSCEPEKRLFLWENILLVGGCSLIRGIKDRIESELAVLlaaseTSSEYQAKdvkwIKLPDYFVEFKdr 418
Cdd:pfam00022 301 VGIPELIVDAI-NACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQL-----APPGVKVK----IIAPGNTVERR-- 368
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1028571264 419 scDAAFLGGSITAKL-VFtssGAMYLTRADYDEFGP 453
Cdd:pfam00022 369 --YSAWIGGSILASLgTF---QQMWVSKQEYEEHGA 399
PTZ00004 PTZ00004
actin-2; Provisional
86-455 3.16e-49

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 172.26  E-value: 3.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  86 MMVDSPSHAVVANTATTTVSPAAVADELRVN-----TRHDANESGKGSAS------DHASS-----AWVQPIQNGQVADW 149
Cdd:PTZ00004    1 MSVEETNAAVVDNGSGMVKAGFAGDDAPRCVfpsivGRPKNPGIMVGMEEkdcyvgDEAQDkrgilTLKYPIEHGIVTNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 150 DALQVLWRKILVNHcgVERATNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLVVDIGH 229
Cdd:PTZ00004   81 DDMEKIWHHTFYNE--LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 230 TTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSG--------DEKFVASYGK----YIGKDLArafiqspAFFAPS 297
Cdd:PTZ00004  159 GVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHErgttftttAEKEIVRDIKeklcYIALDFD-------EEMGNS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 298 LSGIEQPNAEFDF-KGQKIDIGSWGFRAIDVLFKPELIGKDVP-GIHDamhLVVS--NSCEPEKRLFLWENILLVGGCSL 373
Cdd:PTZ00004  232 AGSSDKYEESYELpDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHE---LTFQsiNKCDIDIRKDLYGNIVLSGGTTM 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 374 IRGIKDRIESELAVLLAASETSSEYQAKDVKwiklpdyfvefkdrscDAAFLGGSITAKLvfTSSGAMYLTRADYDEFGP 453
Cdd:PTZ00004  309 YRGLPERLTKELTTLAPSTMKIKVVAPPERK----------------YSVWIGGSILSSL--PTFQQMWVTKEEYDESGP 370

                  ..
gi 1028571264 454 AA 455
Cdd:PTZ00004  371 SI 372
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
139-452 5.48e-48

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: 168.52  E-value: 5.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 139 QPIQNGQVADWDALQVLWRKILVNHCGVEraTNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAG 218
Cdd:cd13397    64 YPIEHGIVTNWDDMEKIWHHTFENELRVK--PEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 219 VTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLM--SGDeKFVASYGKYIGKDLARAFIQSPAFFAP 296
Cdd:cd13397   142 RTTGLVLDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLkeRGH-SFTTTAEREIVRDIKEKLCYVALDYEE 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 297 SLSGIEQPNAEfDFK---GQKIDIGSWGFRAIDVLFKPELIGKDVPGIHdamHLVVS--NSCEPEKRLFLWENILLVGGC 371
Cdd:cd13397   221 ELKKKSEELEK-EYTlpdGQVIKIGSERFRCPEALFRPSLIGREAPGIH---KLVYNsiMKCDIDIRKDLYSNIVLSGGS 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 372 SLIRGIKDRIESELAVLLAASETsseyqakdVKWIKLPdyfvefkDRsCDAAFLGGSITAKLvfTSSGAMYLTRADYDEF 451
Cdd:cd13397   297 TMFPGLPERLQKELEALAPSSTK--------VKVIAPP-------ER-KYSVWIGGSILASL--STFKSMWITRAEYDEF 358

                  .
gi 1028571264 452 G 452
Cdd:cd13397   359 G 359
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
138-452 1.72e-42

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: 155.03  E-value: 1.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 138 VQPIQNGQVADWDALQVLWRKILVNHCGVEraTNINPVLLTVPvSW-SRSDQERATRILFEYINVPGMFLLDQPVAALYG 216
Cdd:cd13395    74 ISPLKDGLIEDWDAFEKLWDHALKNRLRVD--PSEHPLLLTEP-SWnTRANREKLTELMFEKYNVPAFFLAKNAVLSAFA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 217 AGVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSGDE-KFVASYG-------------KYIGKD 282
Cdd:cd13395   151 NGRSTALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNiEIIPRYMikskepveggapaKYTKKD 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 283 LA-----------RAFIQ---------SPAFFAPSLSGiEQPNAEFDF-KGQKIDIGSWGFRAIDVLFKPELI------- 334
Cdd:cd13395   231 LPnttssyhrymvRRVLQdfkesvcqvSDSPFDESEAA-SIPTVSYELpDGYNIEFGAERFKIPELLFDPSLVkgipapp 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 335 --GKDVPGIHdamHLVVS--NSCEPEKRLFLWENILLVGGCSLIRGIKDRIESELAVLLAASetsseyqakdVKwIKL-- 408
Cdd:cd13395   310 seGNELLGLP---QLVYTsiGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGS----------LK-LKIla 375
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1028571264 409 PDYFVEfkdRSCdAAFLGGSITAKLvftssGA---MYLTRADYDEFG 452
Cdd:cd13395   376 SGNTVE---RRF-SSWIGGSILASL-----GSfqqMWISKQEYEEHG 413
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
140-454 1.83e-39

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: 145.97  E-value: 1.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 140 PIQNGQVADWDALQVLWRKILVNHCGVerATNINPVLLT-VPVSwSRSDQERATRILFEYINVPGMFLLDQPVAALYGAG 218
Cdd:cd10224    65 PIEHGIVTNWDDMEKIWHHTFYNELRV--APEEHPVLLTeAPLN-PKANREKMTQIMFETFNVPAMYVAIQAVLSLYASG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 219 VTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSgdEK---FVASYGKYIGKDL-------ARAFI 288
Cdd:cd10224   142 RTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILT--ERgysFTTTAEREIVRDIkeklcyvALDFE 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 289 QSPAFFAPSlSGIEQPNAEFDfkGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHlvvsNS---CEPEKRLFLWENI 365
Cdd:cd10224   220 QEMQTAASS-SSLEKSYELPD--GQVITIGNERFRCPEALFQPSFLGMEAAGIHETTY----NSimkCDVDIRKDLYANI 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 366 LLVGGCSLIRGIKDRIESELAVLLAASETsseyqakdVKWIKLPD--YFVefkdrscdaaFLGGSITAKLvfTSSGAMYL 443
Cdd:cd10224   293 VLSGGTTMFPGIADRMQKEITALAPSTMK--------IKIVAPPErkYSV----------WIGGSILASL--STFQQMWI 352
                         330
                  ....*....|.
gi 1028571264 444 TRADYDEFGPA 454
Cdd:cd10224   353 SKQEYDESGPS 363
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
140-455 5.25e-38

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: 141.91  E-value: 5.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 140 PIQNGQVADWDALQVLWRKILVNHcgvERATNI--NPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGA 217
Cdd:cd10216    66 PMEHGIVTDWNDMERIWQYVYSKL---QLNTFSeeHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYAS 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 218 GVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLM--SGdEKFVASygkyIGKDLARAFIQSPAFFA 295
Cdd:cd10216   143 GRTTGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLrkSG-YNFHTS----AEFEIVREIKEKACYVA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 296 PSLSGIEQPNAEFDFK-------GQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDamhlVVSNS---CEPEKRLFLWENI 365
Cdd:cd10216   218 LNPQKEEKLEEEKTEKaqytlpdGSTIEIGPERFRAPEILFNPELIGLEYPGVHE----VLVDSiqkSDLDLRKTLYSNI 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 366 LLVGGCSLIRGIKDRIESELAVLlaasetsseyQAKDVKwIKL---PD--YfvefkdrscdAAFLGGSITAKL-VFTSsg 439
Cdd:cd10216   294 VLSGGSTLFKGFGDRLLSEVKKL----------APKDVK-IRIsapPErlY----------STWIGGSILASLsTFKK-- 350
                         330
                  ....*....|....*.
gi 1028571264 440 aMYLTRADYDEFGPAA 455
Cdd:cd10216   351 -MWVSKKEYEEDGARI 365
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
125-453 3.15e-36

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: 137.17  E-value: 3.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 125 GKGSASDHASSAWVQPIQNGQVADWDALQVLWRKILvnHCGVERATNINPVLLTVPVSWSRSDQERATRILFEYINVPGM 204
Cdd:cd10214    53 GKELANVEPPLKLVNPLRHGIVVDWDCVQDIWEYIF--EKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAM 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 205 FLLDQPVAALYGAGVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLM-SGDEKFVASyGKYIGKDl 283
Cdd:cd10214   131 HIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLnEAGNKFTDD-QLHIVED- 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 284 arafIQSPAFFAPSLSGIEQPNAEFDFK-------GQKIDIGSWGFRAIDVLFKPELIGKDVPGIHD-AMHLVvsNSCEP 355
Cdd:cd10214   209 ----IKKKCCYVALDFEEEMGLPPQEYTvdyelpdGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTlTMNSL--NKCDA 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 356 EKRLFLWENILLVGGCSLIRGIKDRIESELAVLLAASETSSEYQA--KDVKWIklpdyfvefkdrscdaaflGGSITAKL 433
Cdd:cd10214   283 NLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPNDNPIVAASPerKYSVWT-------------------GGSILASL 343
                         330       340
                  ....*....|....*....|
gi 1028571264 434 vfTSSGAMYLTRADYDEFGP 453
Cdd:cd10214   344 --KSFQQLWVRRREYEERGP 361
PTZ00281 PTZ00281
actin; Provisional
79-454 8.99e-35

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 133.29  E-value: 8.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  79 QDTDATDMMVDSPSHAVVANTATTTvSPAAVADELRVNTRHDANESGKGS----ASDHASS-----AWVQPIQNGQVADW 149
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDD-APRAVFPSIVGRPRHTGVMVGMGQkdsyVGDEAQSkrgilTLKYPIEHGIVTNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 150 DALQVLWRKILVNHCGVerATNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLVVDIGH 229
Cdd:PTZ00281   81 DDMEKIWHHTFYNELRV--APEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 230 TTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSG-DEKFVASYGKYIGKDLARAFIQSPAFF------APSLSGIE 302
Cdd:PTZ00281  159 GVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTErGYSFTTTAEREIVRDIKEKLAYVALDFeaemqtAASSSALE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 303 QPNAEFDfkGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHLVVSNsCEPEKRLFLWENILLVGGCSLIRGIKDRIE 382
Cdd:PTZ00281  239 KSYELPD--GQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMK-CDVDIRKDLYGNVVLSGGTTMFPGIADRMN 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028571264 383 SELAVLLAASetsseyqaKDVKWIKLPDYFVefkdrscdAAFLGGSITAKLvfTSSGAMYLTRADYDEFGPA 454
Cdd:PTZ00281  316 KELTALAPST--------MKIKIIAPPERKY--------SVWIGGSILASL--STFQQMWISKEEYDESGPS 369
PTZ00452 PTZ00452
actin; Provisional
94-454 4.84e-34

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 131.42  E-value: 4.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  94 AVVANTATTTVSPAAVA----DELRVNTRHDANESGKGSASDHASSAWVQPIQNGQVADWDALQVLWRKILVNHCGVerA 169
Cdd:PTZ00452   20 GIAGDDAPTSCFPAIVGrskqNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIWHHAFYNELCM--S 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 170 TNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLVVDIGHTTTDISPVFENVAVYSASVT 249
Cdd:PTZ00452   98 PEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVFEGHQIPQAITK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 250 IAVGGQNIETYLVQLMS---------------GDEKFVASYGKYIGKDLARAFIQSPAFFAPslsgIEQPNaefdfkGQK 314
Cdd:PTZ00452  178 INLAGRLCTDYLTQILQelgysltephqriivKNIKERLCYTALDPQDEKRIYKESNSQDSP----YKLPD------GNI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 315 IDIGSWGFRAIDVLFKPELIGKDVPGIHdamHLVVSN--SCEPEKRLFLWENILLVGGCSLIRGIKDRIESELAVLLAAS 392
Cdd:PTZ00452  248 LTIKSQKFRCSEILFQPKLIGLEVAGIH---HLAYSSikKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQ 324
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028571264 393 ETSSEYQAKDVKWiklpdyfvefkdrscdAAFLGGSITAKLvfTSSGAMYLTRADYDEFGPA 454
Cdd:PTZ00452  325 LKIQVAAPPDRRF----------------SAWIGGSIQCTL--STQQPQWIKRQEYDEQGPS 368
PTZ00466 PTZ00466
actin-like protein; Provisional
140-452 2.40e-29

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 118.51  E-value: 2.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 140 PIQNGQVADWDALQVLWRKIlvnHCGVERATNINPVLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGV 219
Cdd:PTZ00466   77 PINHGIIENWNDMENIWIHV---YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGK 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 220 TSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSGDEKFVASYGKYigkDLARAFIQSPAFFAPSL- 298
Cdd:PTZ00466  154 TNGTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEM---EVVKNMKENCCYVSFNMn 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 299 ---SGIEQPNAEFDFK---GQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDAMHLVVSNsCEPEKRLFLWENILLVGGCS 372
Cdd:PTZ00466  231 kekNSSEKALTTLPYIlpdGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITR-ADMDLRRTLYSHIVLSGGTT 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 373 LIRGIKDRIESELavllaasetsSEYQAKDVKW-IKLPdyfvefKDRSCdAAFLGGSITAKLvfTSSGAMYLTRADYDEF 451
Cdd:PTZ00466  310 MFHGFGDRLLNEI----------RKFAPKDITIrISAP------PERKF-STFIGGSILASL--ATFKKIWISKQEFDEY 370

                  .
gi 1028571264 452 G 452
Cdd:PTZ00466  371 G 371
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
131-452 1.58e-24

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: 104.55  E-value: 1.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 131 DHASSAWVQPIQNGQVADWDALQVLWRKILVNHCGVE--RATNInpvLLTVPVSWSRSDQERATRILFEYINVPGMFLLD 208
Cdd:cd10210    49 DLSGLFYRRPFERGYLVNWDLQRQIWDHLFGKLLLNVdpSDTAL---VLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTT 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 209 QPVAALYGAGVTSG----------LVVDIGHTTTDISPVFENVAVYSASVTIAVGG---QNI--------------ETYL 261
Cdd:cd10210   126 AAALSAFAYLADSEqssssssqccLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGkllTNYlkeiisyrqlnvmdETYL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 262 VQLMSgdEK--FVASygKYIgKDLARA-----------------FIQSPAFFApsLSGIEQPNAEFDFKGQKIDIGSWGF 322
Cdd:cd10210   206 VNQIK--EDlcFVST--DFY-EDLEIAkkkgkentirrdyvlpdYTTSKRGYV--RDPEEPNRGKLKEDEQVLRLNNERF 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 323 RAIDVLFKPELIGKDVPGIHDAMHLVVsNSCEPEKRLFLWENILLVGGCSLIRGIKDRIESELAVLLaasetSSEYqakD 402
Cdd:cd10210   279 TVPELLFHPSDIGIQQAGIAEAIVQSI-NACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLA-----PDDY---D 349
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1028571264 403 VKwIKLPDyfvefkDRSCdAAFLGGSItaklvFTSSGA---MYLTRADYDEFG 452
Cdd:cd10210   350 VN-VTLPE------DPIT-YAWEGGSL-----LAQSPEfeeLAVTRAEYEEHG 389
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
172-450 5.39e-23

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: 100.02  E-value: 5.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 172 INP----VLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLVVDIGHTTTDISPVFENVAVYSAS 247
Cdd:cd10207    68 VNPkdrrVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYEGVPLLSAW 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 248 VTIAVGG----QNIETYL-----VQLMSGDEKFVASYGKYIGKD-----LARA-FIQSP--------AFFAPSLSGIEQP 304
Cdd:cd10207   148 QSTPLGGkalhKRLKKLLlehatVVTGDNKGQLLSSVDSLLSEEvlediKVRAcFVTSLergktlqsATEEGSTEEPSPP 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 305 NA-EFDFKGQKIDIGSWGFR--AIDVLFKPELIGKDVPgihdamHLVVS--NSCEPEKRLFLWENILLVGGCSLIRGIKD 379
Cdd:cd10207   228 PPvDYPLDGEKILIVPGSIResAEELLFEGDNEEKSLP------TLILDslLKCPIDVRKQLAENIVVIGGTSMLPGFKH 301
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028571264 380 RIESELAVLLAASETSSEYQAKDVKWIKLPDYFVEfkdrSCdAAFLGGSITAKLvfTSSGAMYLTRADYDE 450
Cdd:cd10207   302 RLLEELRALLRKPKYFEELAPKTFRFHTPPSVFKP----NY-LAWLGGSIFGAL--ESILGRSLSREAYLQ 365
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
140-455 1.17e-22

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: 99.18  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 140 PIQNGQVADWDALQVLWrkilvNHCGVERaTNINP----VLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALY 215
Cdd:cd10220    67 PMENGIVRNWDDMEHLW-----DYTFGEK-LKIDPreckILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLY 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 216 GAGVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLM---------SGD--------EKFVasygkY 278
Cdd:cd10220   141 AQGLLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYLIKLLllrgyafnrTADfetvreikEKLC-----Y 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 279 IGKDLARAfiQSPAFFAPSLsgIEQ---PNaefdfkGQKIDIGSWGFRAIDVLFKPELIGKDVPGIHDamhLVVS--NSC 353
Cdd:cd10220   216 VAYDIELE--QKLALETTVL--VESytlPD------GRVIKVGGERFEAPEALFQPHLIDVEGPGIAE---LLFNtiQAA 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 354 EPEKRLFLWENILLVGGCSLIRGIKDRIEselavllaasetsseyqaKDVKWIKL-------PDYFVEFKDRSCDAA--- 423
Cdd:cd10220   283 DIDTRPELYKHIVLSGGSTMYPGLPSRLE------------------KEIKQLYLervlkgdTERLSKFKIRIEDPPrrk 344
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1028571264 424 ---FLGGSITAKLVfTSSGAMYLTRADYDEFGPAA 455
Cdd:cd10220   345 hmvFLGGAVLADIM-KDKDEFWITRQEYEEQGVRV 378
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
98-453 4.01e-21

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 95.18  E-value: 4.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  98 NTATTTVSPAAVAD--ELRVNTRHDANES-----GKGSASDHASSAWVQPIQNGQVADWDALQVLWRKILVNHCGVErat 170
Cdd:PTZ00280   23 NTEPTYIIPTLIADnsKQSRRRSKKGFEDldfyiGDEALAASKSYTLTYPMKHGIVEDWDLMEKFWEQCIFKYLRCE--- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 171 ninP----VLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYGA----------GVTSGLVVDIGHTTTDISP 236
Cdd:PTZ00280  100 ---PeehyFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVIDSGDGVTHVIP 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 237 VFENVAVYSASVTIAVGGQNIETYLVQLM--------SGDEKFVASYGK----YIGKDLARAF---IQSPAffapslSGI 301
Cdd:PTZ00280  177 VVDGYVIGSSIKHIPLAGRDITNFIQQMLrergepipAEDILLLAQRIKekycYVAPDIAKEFekyDSDPK------NHF 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 302 EQPNAEFDFKGQK--IDIGSWGFRAIDVLFKPELIGKD----VPGIHDAmhlvVSNSCEPEKRLFLWENILLVGGCSLIR 375
Cdd:PTZ00280  251 KKYTAVNSVTKKPytVDVGYERFLGPEMFFHPEIFSSEwttpLPEVVDD----AIQSCPIDCRRPLYKNIVLSGGSTMFK 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 376 GIKDRIESELAVLL--------AASETSSEYQAKDVKWIKLPdyfvefkdRSCDAAFLGGSITAKL-VFTSsgaMYLTRA 446
Cdd:PTZ00280  327 GFDKRLQRDVRKRVdrrlkkaeELSGGKLKPIPIDVNVVSHP--------RQRYAVWYGGSMLASSpEFEK---VCHTKA 395

                  ....*..
gi 1028571264 447 DYDEFGP 453
Cdd:PTZ00280  396 EYDEYGP 402
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
11-455 6.73e-21

nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The Arp8-like family includes Arp8, also called actin-like protein 8, from vertebrates and fungi. Human Arp8 is encoded by the ACTR8 gene and is also known as INO80 complex subunit N. It plays an important role in the functional organization of mitotic chromosomes. Arp8 exhibits low basal ATPase activity, and is unable to polymerize. It is probably a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication, and probably DNA repair. it is required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Arp8 strongly prefers nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. This subfamily also contains Arabidopsis thaliana Arp9.


Pssm-ID: 466812 [Multi-domain]  Cd Length: 447  Bit Score: 94.62  E-value: 6.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  11 NLLVIDPGSLYTRAGLADYQNP--------------PALTAISRISDKELAAELEAQEIAQREALLETQTASKELLLTEQ 76
Cdd:cd10206     1 KTIVIHPGSRNLRIGRASDDLPvviphciarrrkqtGSARPEDVPPAVRNGEDSVESEEEREEALKEVERALKSRKKSNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  77 TAqdtdatdmmvdSPSHAVVANTATTT--VSPAAVADELRVNTRHDANESGK---GSASDH--ASSAWV--QPIQNGQVA 147
Cdd:cd10206    81 RR-----------RIPNQVSAKQNKPSkpENVPEDLDASSGENWTDTSDYPDflvGEEALRlpPSEEYNlhWPIRRGRLN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 148 DW----------DALQVLWRKILVNHCGVERAT--NINPVLLtVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALY 215
Cdd:cd10206   150 VHsdggsltavlDDLEDIWSHALEEKLEIPRKDlkNYRAVLV-IPDLFDRRHVKELVDLLLRRLGFSSVFVHQESVCATF 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 216 GAGVTSGLVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLM--------------SGDEKFVAS-YGKYIG 280
Cdd:cd10206   229 GAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLrrsgfpyrecnlnsPLDFLLLERlKETYCT 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 281 KDLARAFIQSPAFFapslsgIEQPNAE---FDFKgqkidigswgfraidvlfkpeligkdVPGIHDAmhlVVS--NSCE- 354
Cdd:cd10206   309 LDQDDIGVQLHEFY------VREPGQPtlkYQFK--------------------------LLPLDEA---IVQsiLSCAs 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 355 PEKRLFLWENILLVGGCSLIRGIKDRIESELavllaasetsseyqakdvkWIKLPDYF-----VEF--KDRSCDAAFL-- 425
Cdd:cd10206   354 DELKRKMYSSILLVGGGAKIPGLAEALEDRL-------------------LIKIPSLFeavetVEVlpPPKDMDPSLLaw 414
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1028571264 426 -GGSITAKLvfTSSGAMYLTRADYDEFGPAA 455
Cdd:cd10206   415 kGGAVLACL--DSAQELWITRKEWQRLGVRA 443
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
98-453 1.35e-19

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: 90.32  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  98 NTATTTVSPAAVADELRVNTRHDANESGKG----------SASDHASS-AWVQPIQNGQVADWDALQVLWRKILVNHCGV 166
Cdd:cd10221    18 NTEPQFIIPTVIAIKESAKVGDGQRRSKKGiedldfyigdEALANSPTyALKYPIRHGIVEDWDLMERFWEQCIFKYLRC 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 167 EratninP----VLLTVPVSWSRSDQERATRILFEYINVPGMFLLDQPVAALYgAGVTS---------GLVVDIGHTTTD 233
Cdd:cd10221    98 E------PedhyFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALA-ASWTSrkvgertltGTVIDSGDGVTH 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 234 ISPVFENVAVYSASVTIAVGGQNIeTYLVQLM---------SGDEKFVASYGK----YIGKDLARAFI---QSPAFFAPS 297
Cdd:cd10221   171 VIPVAEGYVIGSCIKHIPIAGRDI-TYFIQQLlrereegipPEDSLEVAKRIKerycYVCPDIVKEFAkydSDPAKYIKQ 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 298 LSGIEQPNaefdfkGQK--IDIGSWGFRAIDVLFKPELIGKD-VPGIHDAMHLVVSnSCEPEKRLFLWENILLVGGCS-- 372
Cdd:cd10221   250 YTGINSVT------GKPytVDVGYERFLAPEIFFNPEIASSDfTTPLPEVVDQVIQ-SCPIDTRRGLYKNIVLSGGSTmf 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 373 ------LIRGIKDRIESELAVLLAASETSSEYQAKDVKWIKLPdyfvefKDRScdAAFLGGSITAklvftSSGAMY---L 443
Cdd:cd10221   323 kdfgrrLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHP------MQRY--AVWFGGSMLA-----STPEFYtvcH 389
                         410
                  ....*....|
gi 1028571264 444 TRADYDEFGP 453
Cdd:cd10221   390 TKAEYEEYGP 399
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
162-453 6.23e-18

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: 84.55  E-value: 6.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 162 NHCGVERATNI-NPVLLTVPV---SWSRSdqeRATRILFEYINVPG-MFLLDqpvaALY-------GAGVTSGLVVDIGH 229
Cdd:cd10211    82 SHLGINSEGSVdHPIVLTEALcnpNYSRQ---LMSELLFECYGVPSvAYGID----SLFsyyhnqpQGDPSDGLVISSGY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 230 TTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMSgdekfvasyGKYigkdlarafiqsPAFFAP-SLSGIEQPNAEF 308
Cdd:cd10211   155 STTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQ---------LKY------------PTHPSAiTLSRAEELVHEH 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 309 -----DFKgqkidigswgfRAIDVLFKPELIGKDV------PGIHDAMHLVVSNSCePEKRLFLWENILLVGGCSLIRGI 377
Cdd:cd10211   214 cyvaeDYD-----------EELKKWEDPEYYEENVrkiqlpFGLVETIEFVLKRYP-AEQQDRLVQNVFLTGGNALFPGL 281
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028571264 378 KDRIESELAVLLAASETSSEYQAKDVkwiklpdyfvefkdrSCDaAFLGGSITAKLVFTSSGAMylTRADYDEFGP 453
Cdd:cd10211   282 KERLEKELRAIRPFGSPFNVVRAKDP---------------VLD-AWRGAAKWALDSTFEKVWI--TKQEYEEKGG 339
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
174-392 3.44e-15

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: 76.43  E-value: 3.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 174 PVLLTVPVSWS-RSDQERATR---------ILFEyINVPGMFLLDQPVAALYGAGVTSGLVVDIGHTTTDISPVFENVAV 243
Cdd:cd13396    60 PVVVSLPLCHSdDTESAAASRrqlrgtifnVLFD-MNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTTIVPVYRGRVM 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 244 YSASV-TIAVGGQNIETYLVQLMSGDE-KFVASYG-KYIGKDLARAFIQSPAFFAPSLSGIEQpnaefDFKGQKIDIGSW 320
Cdd:cd13396   139 HDIGVeVVGQGALRLTGFLKELMQQNGiRFPSLYTvRTIKEKLCYVAEDYEAELAKDTQASCE-----VAGEGWFTLSNE 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028571264 321 GFRAIDVLFKPELIGKDVPGIHDAM-----HLVVSNSCEPEKrlflW-ENILLVGGCSLIRGIKDRIESELAVLLAAS 392
Cdd:cd13396   214 RFKTGEILFQPGLGGMRAMGLHQAValcmdHCALVHSQGDDG----WfKTIVLSGGSACLPGLSERLERELRKLLPKS 287
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
148-387 4.83e-10

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: 61.27  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 148 DWDALQVLWRKILVNHCGVerATNINPVLLTVPVSWSRSDQ---ERATRILFEYINVPGMFLLDQPVAALYGAGVTSGLV 224
Cdd:cd10212    77 NWDALEMQWRYLYDTQLKV--SPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFV 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 225 VDIGHTTTDISPVFENVAVYSASVTIAVGGQ----NIETYLVQLMSGD------------------------EKFVASYG 276
Cdd:cd10212   155 IDIGASGCNVTPIIDGIVVKNAVVRSKFGGDfldfQVHERLAPLIKEEndmenmadeqkrstdvwyeastwiQQFKSTML 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 277 KYIGKD---LARAFIQSPAFFAPSLSGIEQPNAEFDF-----------------------KGQKIDIGSWgFRAIDVLFK 330
Cdd:cd10212   235 QVSEKDlfeLERYYKEQADIYAKQQEQLKQMDQQLQYtaltgspnnplvqkknflfkplnKTLTLDLKEC-YQFAEYLFK 313
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 331 PELIgKDVPGIHDAMHLVVSNSCE--PEKRL-FLWENILLVGGCSLIRGIKDRIESELAV 387
Cdd:cd10212   314 PQLI-SDKFSPEDGLGPLMAKSVKkaPEQVYsLLLTNVIITGSTSLIEGMEQRIIKELSI 372
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
99-386 6.42e-08

nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 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: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 54.03  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264  99 TATTTVSPAAVADELRVNTRHDANESGKGSASDHASSAwVQPIQngqvadwDALQVLWRKILVNHCGVERATNINP--VL 176
Cdd:cd10170     7 TTYSGVAYALLGPGEPPLVVLQLPWPGGDGGSSKVPSV-LEVVA-------DFLRALLEHAKAELGDRIWELEKAPieVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 177 LTVPVSWSRSDQER----ATRILFEYINvPGMFLLDQPVAALYGAGVTSG-----------LVVDIGHTTTDISpVFENV 241
Cdd:cd10170    79 ITVPAGWSDAAREAlreaARAAGFGSDS-DNVRLVSEPEAAALYALEDKGdllplkpgdvvLVCDAGGGTVDLS-LYEVT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 242 AVY-------SASVTIAVGGQNI----ETYLVQLMSGDEKFVASYGKYIGKDLARAFIQSPAffapSLSGIEQPNAEFDF 310
Cdd:cd10170   157 SGSpllleevAPGGGALLGGTDIdeafEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKK----RFSGGEEDERLVPS 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028571264 311 KGQKIDIgSWGFRAIDVLFKPELIgKDV--PGIHDAMHLVVSNSCEPEKRLFlwENILLVGGCSLIRGIKDRIESELA 386
Cdd:cd10170   233 LLGGGLP-ELGLEKGTLLLTEEEI-RDLfdPVIDKILELIEEQLEAKSGTPP--DAVVLVGGFSRSPYLRERLRERFG 306
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
138-387 2.19e-07

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: 52.48  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 138 VQPIQNGQVADWDALqvlwrKILVNHCgVERATN----INP-VLLTVPvsWSRSDQERatRILFEYINVPGM---FLLDQ 209
Cdd:cd10225    58 IRPLRDGVIADFEAT-----EAMLRYF-IRKAHRrrgfLRPrVVIGVP--SGITEVER--RAVKEAAEHAGArevYLIEE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 210 PVAALYGAGV-----TSGLVVDIGHTTTDISPVFENVAVYSASVTIAvggqnietylvqlmsGDE------KFV-ASYGK 277
Cdd:cd10225   128 PMAAAIGAGLpieepRGSMVVDIGGGTTEIAVISLGGIVTSRSVRVA---------------GDEmdeaiiNYVrRKYNL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 278 YIGKDLA-RAFIQSPAFFAPslsgieQPNAEFDFKG--------QKIDIGSWGFRaidvlfkpELIGKDVPGIHDAMHLV 348
Cdd:cd10225   193 LIGERTAeRIKIEIGSAYPL------DEELSMEVRGrdlvtglpRTIEITSEEVR--------EALEEPVNAIVEAVRST 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1028571264 349 VSnSCEPEKRLFLWEN-ILLVGGCSLIRGIKDRIESELAV 387
Cdd:cd10225   259 LE-RTPPELAADIVDRgIVLTGGGALLRGLDELLREETGL 297
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
138-386 8.34e-06

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: 47.59  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 138 VQPIQNGQVADWD-----ALQVLWRKILvNHCGVERATNINPVLlTVPVSWSRSDQERATRILFEYINvpGMFLLDQPVA 212
Cdd:cd24009    61 RRPLEDGVIKEGDdrdleAARELLQHLI-ELALPGPDDEIYAVI-GVPARASAENKQALLEIARELVD--GVMVVSEPFA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 213 ALYGAG-VTSGLVVDIGHTTTDISpvfenvAVYSA------SVTIAVGGQNIETYLVQLMsgDEKFVASYgkyIGKDLAR 285
Cdd:cd24009   137 VAYGLDrLDNSLIVDIGAGTTDLC------RMKGTipteedQITLPKAGDYIDEELVDLI--KERYPEVQ---LTLNMAR 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 286 AFIQSPAFFAPSLSGIEqpnAEFDFKG--QKIDIGswgfraidvlfkPELI---GKDVPGIHDAMHLVVSnSCEPEKRLF 360
Cdd:cd24009   206 RWKEKYGFVGDASEPVK---VELPVDGkpVTYDIT------------EELRiacESLVPDIVEGIKKLIA-SFDPEFQEE 269
                         250       260
                  ....*....|....*....|....*.
gi 1028571264 361 LWENILLVGGCSLIRGIKDRIESELA 386
Cdd:cd24009   270 LRNNIVLAGGGSRIRGLDTYIEKALK 295
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
205-387 2.74e-05

MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.


Pssm-ID: 399596 [Multi-domain]  Cd Length: 327  Bit Score: 46.01  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 205 FLLDQPVAALYGAGV-----TSGLVVDIGHTTTDispvfenVAVYSA-----SVTIAVGGQNIETYLVQLMSgdekfvAS 274
Cdd:pfam06723 125 FLIEEPMAAAIGAGLpveepTGNMVVDIGGGTTE-------VAVISLggivtSKSVRVAGDEFDEAIIKYIR------KK 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 275 YGKYIGKDLARAfIQspaffapslsgIEQPNAEFDFKGQKIDIgswgfRAIDVLF-KP-----------ELIGKDVPGIH 342
Cdd:pfam06723 192 YNLLIGERTAER-IK-----------IEIGSAYPTEEEEKMEI-----RGRDLVTgLPktieisseevrEALKEPVSAIV 254
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1028571264 343 DAMHLVVSNsCEPEKRLFLWEN-ILLVGGCSLIRGIKDRIESELAV 387
Cdd:pfam06723 255 EAVKEVLEK-TPPELAADIVDRgIVLTGGGALLRGLDKLLSDETGL 299
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
205-390 3.11e-05

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: 45.84  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 205 FLLDQPVAALYGAGV----TSG-LVVDIGHTTTDIspvfenvAVYS-----ASVTIAVGGQNIETYLVQLMSgdEKfvas 274
Cdd:COG1077   131 YLIEEPMAAAIGAGLpieePTGnMVVDIGGGTTEV-------AVISlggivVSRSIRVAGDELDEAIIQYVR--KK---- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 275 YGKYIG--------KDLARAFiqspaffapslsgIEQPNAEFDFKGQ--------KIDIGSwgfraIDVLfkpELIGKDV 338
Cdd:COG1077   198 YNLLIGertaeeikIEIGSAY-------------PLEEELTMEVRGRdlvtglpkTITITS-----EEIR---EALEEPL 256
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1028571264 339 PGIHDAMHLVVSNsCEPEKRLFLWEN-ILLVGGCSLIRGIKDRIESE--LAVLLA 390
Cdd:COG1077   257 NAIVEAIKSVLEK-TPPELAADIVDRgIVLTGGGALLRGLDKLLSEEtgLPVHVA 310
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
209-266 2.53e-04

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 42.51  E-value: 2.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028571264 209 QPVAALYGAGVTSG-------LVVDIGHTTTDISPVFENVAVYSASVTIAVGGQNIETYLVQLMS 266
Cdd:cd10227   145 EGAGAYLDYLLDDDeledgnvLVIDIGGGTTDILTFENGKPIEESSDTLPGGEEALEKYADDILN 209
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
171-243 4.93e-04

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 42.50  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028571264 171 NINPVLLTVPVSWSRSdQERAT------------RILFEyinvpgmflldqPVAALYGAGVTSG------LVVDIGHTTT 232
Cdd:COG0443   110 PVTRAVITVPAYFDDA-QRQATkdaariaglevlRLLNE------------PTAAALAYGLDKGkeeetiLVYDLGGGTF 176
                          90
                  ....*....|....*..
gi 1028571264 233 DIS------PVFENVAV 243
Cdd:COG0443   177 DVSilrlgdGVFEVLAT 193
ASKHA_NBD_EutJ cd24047
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ...
206-246 1.49e-03

nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.


Pssm-ID: 466897 [Multi-domain]  Cd Length: 241  Bit Score: 39.94  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1028571264 206 LLDQPVAALYGAGVTSGLVVDIGHTTTDISpVFENVAV-YSA 246
Cdd:cd24047    97 VVDEPTAANAVLGIRDGAVVDIGGGTTGIA-VLKDGKVvYTA 137
PRK13927 PRK13927
rod shape-determining protein MreB; Provisional
205-251 3.79e-03

rod shape-determining protein MreB; Provisional


Pssm-ID: 237562 [Multi-domain]  Cd Length: 334  Bit Score: 39.30  E-value: 3.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1028571264 205 FLLDQPVAALYGAGV-----TSGLVVDIGHTTTDISPVFENVAVYSASVTIA 251
Cdd:PRK13927  128 YLIEEPMAAAIGAGLpvtepTGSMVVDIGGGTTEVAVISLGGIVYSKSVRVG 179
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
224-257 4.70e-03

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 37.70  E-value: 4.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1028571264 224 VVDIGHTTTDISpVFENVAVYSASVtIAVGGQNI 257
Cdd:pfam14450   2 LIDIGGGTTDIA-VFEDGALRHTRV-IPVGGNGI 33
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
209-257 6.73e-03

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 38.58  E-value: 6.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028571264 209 QPVAALYGA--------GVTsglVVDIGHTTTDISpVF-ENVAVYSASvtIAVGGQNI 257
Cdd:COG0849   184 SPLASAEAVltedekelGVA---LVDIGGGTTDIA-VFkDGALRHTAV--IPVGGDHI 235
 
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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