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Conserved domains on  [gi|2099366621|ref|NP_001008446|]
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actin-related protein 5 [Gallus gallus]

Protein Classification

COG5277 family protein( domain architecture ID 10009158)

COG5277 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
33-572 0e+00

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: 568.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGARGGAgAETQVGNDLGSPEPLRWLLRSPFDRNVPVQLELQE 112
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDK-----EPRLVFRNLVAKPRDRKKGI-TVTLVGNDILNDEAVRSHLRSPFDRNVVTNFDLQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 113 LLFDHVFQRLGVASQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNWPCSGLVISSGY 192
Cdd:cd10211    75 QILDYIFSHLGINSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQGDPSDGLVISSGY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 193 QCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKYPGHFAAITLSRMEEILHEHSYIAEDYTEELQKWRSPEYYE 272
Cdd:cd10211   155 STTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 273 NNVHKMQLPFsnkllgstltseekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelledgqmdqfhkalveln 352
Cdd:cd10211   235 ENVRKIQLPF---------------------------------------------------------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 353 mdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplsseqsledvesinefeplfaeeqpeaekpva 432
Cdd:cd10211       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 433 avqpvfnlaeyhqlflgterirapeiifqpsligedqtGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLKARVQ 512
Cdd:cd10211   245 --------------------------------------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 513 KELLEMRPFQSSFQVHLASSPILDAWHGARDWAVEHmTREEGWITRKDYEEKGGEYLKEH 572
Cdd:cd10211   287 KELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDS-TFEKVWITKQEYEEKGGEYLKEH 345
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
401-515 4.59e-03

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


The actual alignment was detected with superfamily member cd10208:

Pssm-ID: 483947  Cd Length: 356  Bit Score: 39.60  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 401 LSSEQSLEDVESINEFEPLFaeEQPEAEKPVAAVQPV---FNLAEYHQLFLGTERIRAPEIIFQPSLIGEDqTGIAETMQ 477
Cdd:cd10208   163 LKSDEPELKSQAESGEEATL--DLAEALKKSPICEVLsdgADLASGTEITVGKERFRACEPLFKPSSLRVD-LLIAAIAG 239
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2099366621 478 YVLERYSKE--QQALLVQNVFLTGGNAMYPGLKARVQKEL 515
Cdd:cd10208   240 ALVLNASDEpdKRPALWENIIIVGGGSRIRGLKEALLSEL 279
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
33-572 0e+00

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: 568.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGARGGAgAETQVGNDLGSPEPLRWLLRSPFDRNVPVQLELQE 112
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDK-----EPRLVFRNLVAKPRDRKKGI-TVTLVGNDILNDEAVRSHLRSPFDRNVVTNFDLQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 113 LLFDHVFQRLGVASQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNWPCSGLVISSGY 192
Cdd:cd10211    75 QILDYIFSHLGINSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQGDPSDGLVISSGY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 193 QCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKYPGHFAAITLSRMEEILHEHSYIAEDYTEELQKWRSPEYYE 272
Cdd:cd10211   155 STTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 273 NNVHKMQLPFsnkllgstltseekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelledgqmdqfhkalveln 352
Cdd:cd10211   235 ENVRKIQLPF---------------------------------------------------------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 353 mdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplsseqsledvesinefeplfaeeqpeaekpva 432
Cdd:cd10211       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 433 avqpvfnlaeyhqlflgterirapeiifqpsligedqtGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLKARVQ 512
Cdd:cd10211   245 --------------------------------------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 513 KELLEMRPFQSSFQVHLASSPILDAWHGARDWAVEHmTREEGWITRKDYEEKGGEYLKEH 572
Cdd:cd10211   287 KELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDS-TFEKVWITKQEYEEKGGEYLKEH 345
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
33-565 4.91e-44

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 161.27  E-value: 4.91e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621   33 PLVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGARGGAGA--ETQVGNDLGSPEPLrWLLRSPFDRNVPVQLEL 110
Cdd:smart00268   3 AIVIDNGSGTIKAGFAGED-----FPQVVFPSIVGRPKDGKGMVGDakDIFVGDEAQEKRGG-LELKYPIENGIVENWDD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  111 QELLFDHVFQR-LGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNwpcsGLVIS 189
Cdd:smart00268  77 MEKIWDYTFFNeLRVEPE---EHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTT----GLVID 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  190 SGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQlkypghFAAITLSRMEE------ILHEHSYIAEDYTEELQ 263
Cdd:smart00268 150 SGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLS------ERGYQFNSSAEfeivreIKEKLCYVAEDFEKEMK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  264 KWRspeyyennvhkmqlpfsnkllgstltseekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelledgqmdq 343
Cdd:smart00268 224 LAR----------------------------------------------------------------------------- 226
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  344 fhkalvelnmdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplSSEQSLEDVESinefeplfaee 423
Cdd:smart00268 227 ----------------------------------------------------------ESSESSKLEKT----------- 237
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  424 qpeaekpvaavqpvFNLAEYHQLFLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAM 503
Cdd:smart00268 238 --------------YELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTL 303
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099366621  504 YPGLKARVQKELLEMRPFQSSFQVHLASSPILDAWHGARDWAvEHMTREEGWITRKDYEEKG 565
Cdd:smart00268 304 IPGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILA-SLSTFEDMWITKKEYEESG 364
Actin pfam00022
Actin;
33-565 7.16e-31

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 124.72  E-value: 7.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADPsvpaePLLRFRSLAARSRGARGGAGAETQVGNDLGSPEPLrWLLRSPFDRNVPVQLELQE 112
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDA-----PKAVIPSCVGKPRGTKVEAANKYYVGDEALTYRPG-MEVRSPVEDGIVVDWDAME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 113 LLFDHVF-QRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNwpcsGLVISSG 191
Cdd:pfam00022  77 EIWEHVLkEELQVDPE---EHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTT----GLVVDSG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 192 YQCTHILPVLEGRLDAKNCKRINLGGcqaavylqrllqlkypghfaaitlsrmeeilhehsyiaEDYTEELQKWrspeyy 271
Cdd:pfam00022 150 AGVTSVVPVHDGYVLQKAIRRSDLGG--------------------------------------DFLTDYLREL------ 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 272 ennvhkmqlpFSNKLLGSTLTSEEKQERRQQQLRRLQELNARRREEKLQLDQERldrllyvqELLEDgqmdqFHKALVEL 351
Cdd:pfam00022 186 ----------LRSRNIEITPRYLIKSKKPGDPAPAVTKRELPDTTYSYKTYQER--------RVLEE-----IKESVCYV 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 352 NmdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdLDPlsseqsledvesinefeplFAEEQPEAEKPv 431
Cdd:pfam00022 243 S---------------------------------------------DDP-------------------FGDETTSSSIP- 257
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 432 aavQPVFNLAEYHQLFLGTERIRAPEIIFQPSLIGEDQT--------GIAETMQYVLERYSKEQQALLVQNVFLTGGNAM 503
Cdd:pfam00022 258 ---TRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIVVTGGNSL 334
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099366621 504 YPGLKARVQKELLEMRPFQSSFQVH---LASSPILDAWHGARDWA----VEHMtreegWITRKDYEEKG 565
Cdd:pfam00022 335 FPGFTERLEKELAQLAPPGVKVKIIapgNTVERRYSAWIGGSILAslgtFQQM-----WVSKQEYEEHG 398
PTZ00004 PTZ00004
actin-2; Provisional
34-565 5.25e-25

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 107.16  E-value: 5.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGAR---GGAGAETQVGNDLGSPEPLRWLLRsPFDRNVPVQLEL 110
Cdd:PTZ00004    9 AVVDNGSGMVKAGFAGDD-----APRCVFPSIVGRPKNPGimvGMEEKDCYVGDEAQDKRGILTLKY-PIEHGIVTNWDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 111 QELLFDHVF-QRLGVASqgcVDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRqnwpCSGLVIS 189
Cdd:PTZ00004   83 MEKIWHHTFyNELRVAP---EEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGR----TTGIVLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 190 SGYQCTHILPVLEGRLDAKNCKRINLGGcqaavylqrllqlkypghfaaitlsrmeeilhehsyiaEDYTEELQKWRSPe 269
Cdd:PTZ00004  156 SGDGVSHTVPIYEGYSLPHAIHRLDVAG--------------------------------------RDLTEYMMKILHE- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 270 yyennvhkmqlpfsnklLGSTLTSeekqerrqqqlrrlqelNARRreeklqldqerlDRLLYVQElledgqmdqfhkALV 349
Cdd:PTZ00004  197 -----------------RGTTFTT-----------------TAEK------------EIVRDIKE------------KLC 218
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 350 ELNMDSAEElqsyinklslaieqtkqkilqaevnievdvvdskpetpdldPLSSEQSLEDVESINEfeplfaeeqpeaek 429
Cdd:PTZ00004  219 YIALDFDEE-----------------------------------------MGNSAGSSDKYEESYE-------------- 243
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 430 pvaavqpvfnLAEYHQLFLGTERIRAPEIIFQPSLIGEDQT-GIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLK 508
Cdd:PTZ00004  244 ----------LPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLP 313
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2099366621 509 ARVQKELLEMRPfqSSFQVHLASSP--ILDAWHGARDWAvEHMTREEGWITRKDYEEKG 565
Cdd:PTZ00004  314 ERLTKELTTLAP--STMKIKVVAPPerKYSVWIGGSILS-SLPTFQQMWVTKEEYDESG 369
COG5277 COG5277
Actin-related protein [Cytoskeleton];
451-563 8.29e-04

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 42.08  E-value: 8.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 451 ERIRAPEIIFQPSLIG------------EDQT----------GIAETMQYVLERYSKEQQALLVQNVFLTGGNAMY---P 505
Cdd:COG5277   279 ERFLIGEILFNPNHEGfesyiqqgrlriEDAVigdvvlygemGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpP 358
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099366621 506 GLK-------ARVQKELLEMRPfQSSFQVHLASSPILDAWHGARDWAVE-HMTREEGWITRKDYEE 563
Cdd:COG5277   359 GLEdvavdsvTRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYAlPFSVKWSWITKEGWYF 423
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
401-515 4.59e-03

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: 39.60  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 401 LSSEQSLEDVESINEFEPLFaeEQPEAEKPVAAVQPV---FNLAEYHQLFLGTERIRAPEIIFQPSLIGEDqTGIAETMQ 477
Cdd:cd10208   163 LKSDEPELKSQAESGEEATL--DLAEALKKSPICEVLsdgADLASGTEITVGKERFRACEPLFKPSSLRVD-LLIAAIAG 239
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2099366621 478 YVLERYSKE--QQALLVQNVFLTGGNAMYPGLKARVQKEL 515
Cdd:cd10208   240 ALVLNASDEpdKRPALWENIIIVGGGSRIRGLKEALLSEL 279
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
33-572 0e+00

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: 568.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGARGGAgAETQVGNDLGSPEPLRWLLRSPFDRNVPVQLELQE 112
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDK-----EPRLVFRNLVAKPRDRKKGI-TVTLVGNDILNDEAVRSHLRSPFDRNVVTNFDLQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 113 LLFDHVFQRLGVASQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNWPCSGLVISSGY 192
Cdd:cd10211    75 QILDYIFSHLGINSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQGDPSDGLVISSGY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 193 QCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKYPGHFAAITLSRMEEILHEHSYIAEDYTEELQKWRSPEYYE 272
Cdd:cd10211   155 STTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 273 NNVHKMQLPFsnkllgstltseekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelledgqmdqfhkalveln 352
Cdd:cd10211   235 ENVRKIQLPF---------------------------------------------------------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 353 mdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplsseqsledvesinefeplfaeeqpeaekpva 432
Cdd:cd10211       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 433 avqpvfnlaeyhqlflgterirapeiifqpsligedqtGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLKARVQ 512
Cdd:cd10211   245 --------------------------------------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 513 KELLEMRPFQSSFQVHLASSPILDAWHGARDWAVEHmTREEGWITRKDYEEKGGEYLKEH 572
Cdd:cd10211   287 KELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDS-TFEKVWITKQEYEEKGGEYLKEH 345
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
34-565 1.34e-48

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: 174.28  E-value: 1.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAADPSVpaepllRFRSLAARSRGARG--GAGAETQVGNDLGSpepLRWllRSPFDRNVPVQLELQ 111
Cdd:cd10210     2 LVLDNGAYTIKAGFASDDPPR------VIPNCIAKPKSERRrlFGDDQLDECKDLSG---LFY--RRPFERGYLVNWDLQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 112 ELLFDHVFQRLGVaSQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYqvpkvsyGVDSLY-------SFYHNRRQNW--- 181
Cdd:cd10210    71 RQIWDHLFGKLLL-NVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEY-------GFQSLYrttaaalSAFAYLADSEqss 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 182 ----PCSgLVISSGYQCTHILPVLEGRLDAKNCKRINLGGcqaavylqRLL--QLKYPGHFAAITLSR----MEEILHEH 251
Cdd:cd10210   143 ssssQCC-LVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGG--------KLLtnYLKEIISYRQLNVMDetylVNQIKEDL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 252 SYIAEDYTEELQKwrspeyyennvhkmqlpfsnkllgstltseekqerrqqqlrrlqelnARRREEKLQLDQErldrllY 331
Cdd:cd10210   214 CFVSTDFYEDLEI-----------------------------------------------AKKKGKENTIRRD------Y 240
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 332 VqelLEDGQmdqfhkalvelnmdsaeelqsyinklslaieQTKQKILQaevnievDVVDSKPETPDLDplssEQSLEdve 411
Cdd:cd10210   241 V---LPDYT-------------------------------TSKRGYVR-------DPEEPNRGKLKED----EQVLR--- 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 412 sinefeplfaeeqpeaekpvaavqpvfnlaeyhqlfLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALL 491
Cdd:cd10210   273 ------------------------------------LNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLL 316
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099366621 492 VQNVFLTGGNAMYPGLKARVQKELLEMRPFQSSFQVHLASSPILDAWHGARDWAVEHMTREEgWITRKDYEEKG 565
Cdd:cd10210   317 YANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEEL-AVTRAEYEEHG 389
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
33-565 4.91e-44

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 161.27  E-value: 4.91e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621   33 PLVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGARGGAGA--ETQVGNDLGSPEPLrWLLRSPFDRNVPVQLEL 110
Cdd:smart00268   3 AIVIDNGSGTIKAGFAGED-----FPQVVFPSIVGRPKDGKGMVGDakDIFVGDEAQEKRGG-LELKYPIENGIVENWDD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  111 QELLFDHVFQR-LGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNwpcsGLVIS 189
Cdd:smart00268  77 MEKIWDYTFFNeLRVEPE---EHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTT----GLVID 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  190 SGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQlkypghFAAITLSRMEE------ILHEHSYIAEDYTEELQ 263
Cdd:smart00268 150 SGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLS------ERGYQFNSSAEfeivreIKEKLCYVAEDFEKEMK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  264 KWRspeyyennvhkmqlpfsnkllgstltseekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelledgqmdq 343
Cdd:smart00268 224 LAR----------------------------------------------------------------------------- 226
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  344 fhkalvelnmdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplSSEQSLEDVESinefeplfaee 423
Cdd:smart00268 227 ----------------------------------------------------------ESSESSKLEKT----------- 237
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  424 qpeaekpvaavqpvFNLAEYHQLFLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAM 503
Cdd:smart00268 238 --------------YELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTL 303
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099366621  504 YPGLKARVQKELLEMRPFQSSFQVHLASSPILDAWHGARDWAvEHMTREEGWITRKDYEEKG 565
Cdd:smart00268 304 IPGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILA-SLSTFEDMWITKKEYEESG 364
Actin pfam00022
Actin;
33-565 7.16e-31

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 124.72  E-value: 7.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADPsvpaePLLRFRSLAARSRGARGGAGAETQVGNDLGSPEPLrWLLRSPFDRNVPVQLELQE 112
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDA-----PKAVIPSCVGKPRGTKVEAANKYYVGDEALTYRPG-MEVRSPVEDGIVVDWDAME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 113 LLFDHVF-QRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNwpcsGLVISSG 191
Cdd:pfam00022  77 EIWEHVLkEELQVDPE---EHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTT----GLVVDSG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 192 YQCTHILPVLEGRLDAKNCKRINLGGcqaavylqrllqlkypghfaaitlsrmeeilhehsyiaEDYTEELQKWrspeyy 271
Cdd:pfam00022 150 AGVTSVVPVHDGYVLQKAIRRSDLGG--------------------------------------DFLTDYLREL------ 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 272 ennvhkmqlpFSNKLLGSTLTSEEKQERRQQQLRRLQELNARRREEKLQLDQERldrllyvqELLEDgqmdqFHKALVEL 351
Cdd:pfam00022 186 ----------LRSRNIEITPRYLIKSKKPGDPAPAVTKRELPDTTYSYKTYQER--------RVLEE-----IKESVCYV 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 352 NmdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdLDPlsseqsledvesinefeplFAEEQPEAEKPv 431
Cdd:pfam00022 243 S---------------------------------------------DDP-------------------FGDETTSSSIP- 257
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 432 aavQPVFNLAEYHQLFLGTERIRAPEIIFQPSLIGEDQT--------GIAETMQYVLERYSKEQQALLVQNVFLTGGNAM 503
Cdd:pfam00022 258 ---TRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIVVTGGNSL 334
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099366621 504 YPGLKARVQKELLEMRPFQSSFQVH---LASSPILDAWHGARDWA----VEHMtreegWITRKDYEEKG 565
Cdd:pfam00022 335 FPGFTERLEKELAQLAPPGVKVKIIapgNTVERRYSAWIGGSILAslgtFQQM-----WVSKQEYEEHG 398
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
33-565 3.50e-29

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: 118.83  E-value: 3.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGARGGAGAETQ---VGND-LGSPEPLRwlLRSPFDRNVPVQL 108
Cdd:cd13397     2 AVVIDNGSGLIKAGFAGED-----LPRAVFPSVVGRPKYKAVMLGAGQKevyVGDEaQEKRGVLT--LSYPIEHGIVTNW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 109 ELQELLFDHVFQR-LGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQnwpcSGLV 187
Cdd:cd13397    75 DDMEKIWHHTFENeLRVKPE---EHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRT----TGLV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 188 ISSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKypGHFAAITLSR--MEEILHEHSYIAEDYTEELQK- 264
Cdd:cd13397   148 LDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKER--GHSFTTTAEReiVRDIKEKLCYVALDYEEELKKk 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 265 -WRSPEYYEnnvhkmqLPfsnkllgstltseekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelleDGQMdq 343
Cdd:cd13397   226 sEELEKEYT-------LP--------------------------------------------------------DGQV-- 240
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 344 fhkalvelnmdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplsseqsledvesinefeplfaee 423
Cdd:cd13397       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 424 qpeaekpvaavqpvfnlaeyhqLFLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAM 503
Cdd:cd13397   241 ----------------------IKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTM 298
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099366621 504 YPGLKARVQKELLEMRPfqSSFQVHLASSP--ILDAWHGARDWAVEHmTREEGWITRKDYEEKG 565
Cdd:cd13397   299 FPGLPERLQKELEALAP--SSTKVKVIAPPerKYSVWIGGSILASLS-TFKSMWITRAEYDEFG 359
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
34-256 1.16e-28

nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ubiquitous in eukaryotes, and the major component of the actin cytoskeleton; monomeric globular protein (G-actin) reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. F-actin filaments form with the consequent hydrolysis of ATP. Some actin-related proteins (Arps) have roles in cytoskeletal functions, such as actin polymerization (Arp2/3) and dynein motor activity (Arp1). Both conventional actin and specific Arps have been implicated in chromatin remodeling and/or transcription regulation. The actin/ARP family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466810 [Multi-domain]  Cd Length: 258  Bit Score: 114.90  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAADpsvpaEPLLRFrslaarsrgarggagaetqvgndlgspeplrwllrsPFDRnvpvqlelQEL 113
Cdd:cd10169     1 IVIDNGSGTIKAGFAGED-----APRLIF------------------------------------PWDD--------MEK 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 114 LFDHVFQRLGVASQgcVDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQnwpcSGLVISSGYQ 193
Cdd:cd10169    32 IWEHVFYNLLRVDP--EEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRT----TGLVVDSGEG 105
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099366621 194 CTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKYPGHFAAITLSRMEEILHEHSYIAE 256
Cdd:cd10169   106 VTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLCGLHE 168
PTZ00004 PTZ00004
actin-2; Provisional
34-565 5.25e-25

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 107.16  E-value: 5.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGAR---GGAGAETQVGNDLGSPEPLRWLLRsPFDRNVPVQLEL 110
Cdd:PTZ00004    9 AVVDNGSGMVKAGFAGDD-----APRCVFPSIVGRPKNPGimvGMEEKDCYVGDEAQDKRGILTLKY-PIEHGIVTNWDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 111 QELLFDHVF-QRLGVASqgcVDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRqnwpCSGLVIS 189
Cdd:PTZ00004   83 MEKIWHHTFyNELRVAP---EEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGR----TTGIVLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 190 SGYQCTHILPVLEGRLDAKNCKRINLGGcqaavylqrllqlkypghfaaitlsrmeeilhehsyiaEDYTEELQKWRSPe 269
Cdd:PTZ00004  156 SGDGVSHTVPIYEGYSLPHAIHRLDVAG--------------------------------------RDLTEYMMKILHE- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 270 yyennvhkmqlpfsnklLGSTLTSeekqerrqqqlrrlqelNARRreeklqldqerlDRLLYVQElledgqmdqfhkALV 349
Cdd:PTZ00004  197 -----------------RGTTFTT-----------------TAEK------------EIVRDIKE------------KLC 218
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 350 ELNMDSAEElqsyinklslaieqtkqkilqaevnievdvvdskpetpdldPLSSEQSLEDVESINEfeplfaeeqpeaek 429
Cdd:PTZ00004  219 YIALDFDEE-----------------------------------------MGNSAGSSDKYEESYE-------------- 243
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 430 pvaavqpvfnLAEYHQLFLGTERIRAPEIIFQPSLIGEDQT-GIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLK 508
Cdd:PTZ00004  244 ----------LPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLP 313
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2099366621 509 ARVQKELLEMRPfqSSFQVHLASSP--ILDAWHGARDWAvEHMTREEGWITRKDYEEKG 565
Cdd:PTZ00004  314 ERLTKELTTLAP--STMKIKVVAPPerKYSVWIGGSILS-SLPTFQQMWVTKEEYDESG 369
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
33-265 1.70e-22

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: 99.54  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADpsvpaEPLLRFRSLAARSRGAR---GGAGAETQVGNDLgspEPLRWLL--RSPFDRNVPVQ 107
Cdd:cd10216     3 PVVIDNGSGVIKAGFAGDD-----IPKVVFPSYVGRPKHVRvmaGALEGDVFVGPKA---EEHRGLLkiRYPMEHGIVTD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 108 LELQELLFDHVFQR--LGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQnwpcSG 185
Cdd:cd10216    75 WNDMERIWQYVYSKlqLNTFSE---EHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRT----TG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 186 LVISSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQlKYPGHFaaITLSRME---EILHEHSYIAEDYTEEL 262
Cdd:cd10216   148 VVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLR-KSGYNF--HTSAEFEivrEIKEKACYVALNPQKEE 224

                  ...
gi 2099366621 263 QKW 265
Cdd:cd10216   225 KLE 227
PTZ00281 PTZ00281
actin; Provisional
34-573 4.86e-22

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 98.23  E-value: 4.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAADPsvpaePLLRFRSLAARSR--GARGGAGAE-TQVGNDLGSPEPLrWLLRSPFDRNVPVQLEL 110
Cdd:PTZ00281    9 LVIDNGSGMCKAGFAGDDA-----PRAVFPSIVGRPRhtGVMVGMGQKdSYVGDEAQSKRGI-LTLKYPIEHGIVTNWDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 111 QELLFDHVF-QRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQnwpcSGLVIS 189
Cdd:PTZ00281   83 MEKIWHHTFyNELRVAPE---EHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT----TGIVMD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 190 SGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKypGHFAAITLSR--MEEILHEHSYIAEDYTEELQKWRS 267
Cdd:PTZ00281  156 SGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTER--GYSFTTTAEReiVRDIKEKLAYVALDFEAEMQTAAS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 268 PEYYENNvhkMQLPfsnkllgstltseekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelleDGQMdqfhka 347
Cdd:PTZ00281  234 SSALEKS---YELP--------------------------------------------------------DGQV------ 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 348 lvelnmdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplsseqsledvesinefeplfaeeqpea 427
Cdd:PTZ00281      --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 428 ekpvaavqpvfnlaeyhqLFLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGL 507
Cdd:PTZ00281  249 ------------------ITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGI 310
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099366621 508 KARVQKELLEMRPfqSSFQVHLASSP--ILDAWHGARDWAvEHMTREEGWITRKDYEEKGGEYLKEHC 573
Cdd:PTZ00281  311 ADRMNKELTALAP--STMKIKIIAPPerKYSVWIGGSILA-SLSTFQQMWISKEEYDESGPSIVHRKC 375
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
32-565 5.09e-22

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: 98.21  E-value: 5.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  32 VPLVIDNGSFQTRAGWAAADPsvpaePLLRFRSLAARSR--GARGGAGA-ETQVGNDLGSPEPLrWLLRSPFDRNVPVQL 108
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDA-----PRAVFPSIVGRPRhqGVMVGMGQkDSYVGDEAQSKRGI-LTLKYPIEHGIVTNW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 109 ELQELLFDHVF-QRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQnwpcSGLV 187
Cdd:cd10224    75 DDMEKIWHHTFyNELRVAPE---EHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRT----TGIV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 188 ISSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRllqlkypghfaaitlsrmeeILHEHSYiaedyteelqkwrs 267
Cdd:cd10224   148 LDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMK--------------------ILTERGY-------------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 268 peyyennvhkmqlPFSnkllgstlTSEEKQErrqqqlrrlqelnARRREEKlqldqerldrLLYVqelledgqmdqfhkA 347
Cdd:cd10224   194 -------------SFT--------TTAEREI-------------VRDIKEK----------LCYV--------------A 215
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 348 LvelnmDSAEELQSyinklslaieqtkqkilqaevnievdvvdskpetpdldplsseqsledvesinefeplfAEEQPEA 427
Cdd:cd10224   216 L-----DFEQEMQT-----------------------------------------------------------AASSSSL 231
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 428 EKPvaavqpvFNLAEYHQLFLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGL 507
Cdd:cd10224   232 EKS-------YELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGI 304
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 508 KARVQKELLEMRPfqSSFQVHLASSP--ILDAWHGARDWAvEHMTREEGWITRKDYEEKG 565
Cdd:cd10224   305 ADRMQKEITALAP--STMKIKIVAPPerKYSVWIGGSILA-SLSTFQQMWISKQEYDESG 361
PTZ00466 PTZ00466
actin-like protein; Provisional
33-229 8.30e-18

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 85.77  E-value: 8.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAADPsvpaePLLRFRSLAARSRGARGGAGA---ETQVGNdlgSPEPLRWLLR--SPFDRNVPVQ 107
Cdd:PTZ00466   14 PIIIDNGTGYIKAGFAGEDV-----PNLVFPSYVGRPKYKRVMAGAvegNIFVGN---KAEEYRGLLKvtYPINHGIIEN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 108 LELQELLFDHVFQRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQNwpcsGLV 187
Cdd:PTZ00466   86 WNDMENIWIHVYNSMKINSE---EHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTN----GTV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2099366621 188 ISSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQ 229
Cdd:PTZ00466  159 LDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLR 200
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
467-565 4.16e-16

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: 78.30  E-value: 4.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 467 EDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLKARVQKELLEMRPFQSSFQVHLASSPILDAWHGARDWAv 546
Cdd:cd10169   161 EKLCGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKVKVIAPPERKYSAWIGGSILA- 239
                          90
                  ....*....|....*....
gi 2099366621 547 EHMTREEGWITRKDYEEKG 565
Cdd:cd10169   240 SLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
33-570 4.30e-16

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: 80.30  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAAAD------PSVPAEPLLRfrslaarsrgarggagAETQVGN---------DLGSPeplrwlLR 97
Cdd:cd10220     2 VVVCDNGTGFVKCGFAGSNfpehvfPSLVGRPILR----------------AEEKVGDieikdimvgDEASE------LR 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  98 SPFDRNVPVQ------LELQELLFDHVF-QRLGVASQGCvdhPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSL 170
Cdd:cd10220    60 SMLEVTYPMEngivrnWDDMEHLWDYTFgEKLKIDPREC---KILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 171 YSFYHNRRQnwpcSGLVISSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLK-YPGHFAAI--TLSRMEEI 247
Cdd:cd10220   137 LTLYAQGLL----TGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRgYAFNRTADfeTVREIKEK 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 248 LhehSYIAEDYteelqkwrspeyyennvhkmqlpfsnkllgstltseekqerrqqqlrrlqelnarRREEKLQLDQERLD 327
Cdd:cd10220   213 L---CYVAYDI-------------------------------------------------------ELEQKLALETTVLV 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 328 RllyvQELLEDGQMdqfhkalvelnmdsaeelqsyinklslaieqtkqkilqaevnIEVdvvdskpetpdldplsseqsl 407
Cdd:cd10220   235 E----SYTLPDGRV------------------------------------------IKV--------------------- 247
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 408 edvesinefeplfaeeqpeaekpvaavqpvfnlaeyhqlflGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQ 487
Cdd:cd10220   248 -----------------------------------------GGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDT 286
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 488 QALLVQNVFLTGGNAMYPGLKARVQKELLEM---------RPFQSSFQVHLASSPildawhgARdwavEHMT-------- 550
Cdd:cd10220   287 RPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylervlkgdTERLSKFKIRIEDPP-------RR----KHMVflggavla 355
                         570       580
                  ....*....|....*....|....*
gi 2099366621 551 -----REEGWITRKDYEEKGGEYLK 570
Cdd:cd10220   356 dimkdKDEFWITRQEYEEQGVRVLD 380
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
33-565 2.19e-15

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: 78.23  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  33 PLVIDNGSFQTRAGWAA-ADPS-VPAEPLLRFRSLAARSrgarGGAGAETQVGNDLGSPEP-LRwlLRSPFDRNVPVQLE 109
Cdd:cd10214     5 AVIIDLGTGYCKAGFAGqPRPSyVISSTVGKPPQESAKT----GDNRKETFVGKELANVEPpLK--LVNPLRHGIVVDWD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 110 LQELLFDHVFQR-LGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRqnwpCSGLVI 188
Cdd:cd10214    79 CVQDIWEYIFEKeMKILPE---EHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGR----TSGLVV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 189 SSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLL-QLKYPghFAAITLSRMEEILHEHSYIAEDYTEElqkwrs 267
Cdd:cd10214   152 ESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLnEAGNK--FTDDQLHIVEDIKKKCCYVALDFEEE------ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 268 peyyennvhkMQLPFSnkllgstltseekqerrqqqlrrlqelnarrreeKLQLDQErldrllyvqelLEDGqmdqfhka 347
Cdd:cd10214   224 ----------MGLPPQ----------------------------------EYTVDYE-----------LPDG-------- 240
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 348 lvelnmdsaeelqsyinklslaieqtkqkilqaevnievdvvdskpetpdldplsseqsledvesinefeplfaeeqpea 427
Cdd:cd10214       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 428 ekpvaavqpvfnlaeyHQLFLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGL 507
Cdd:cd10214   241 ----------------HLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGF 304
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2099366621 508 KARVQKELLEMRPFQSSfQVHLASSPILDAWHGARDWAvEHMTREEGWITRKDYEEKG 565
Cdd:cd10214   305 PDRFQKELSKLCPNDNP-IVAASPERKYSVWTGGSILA-SLKSFQQLWVRRREYEERG 360
PTZ00452 PTZ00452
actin; Provisional
34-573 1.24e-14

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 75.95  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAADPSVPAEPLLRFRSlaARSRGARGGAGAETQVGNDLGSPEPLrWLLRSPFDRNVPVQLELQEL 113
Cdd:PTZ00452    8 VVIDNGSGYCKIGIAGDDAPTSCFPAIVGRS--KQNDGIFSTFNKEYYVGEEAQAKRGV-LAIKEPIQNGIINSWDDIEI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 114 LFDHVF-QRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHNRRQnwpcSGLVISSGY 192
Cdd:PTZ00452   85 IWHHAFyNELCMSPE---DQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKT----IGLVVDSGE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 193 QCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLkypghfaaitlsrmeeilhehsyiaedyteelqkwrspeyye 272
Cdd:PTZ00452  158 GVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQE------------------------------------------ 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 273 nnvhkmqlpfsnklLGSTLTSEekqerrqqqlrrlqelnarrreeklqldqerldrllyvqelledgqmdqfHKALVELN 352
Cdd:PTZ00452  196 --------------LGYSLTEP--------------------------------------------------HQRIIVKN 211
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 353 MdsaEELQSYInklslAIEQTKQKILQAEVNIEvdvvDSKPETPDLDPLSseqsledvesinefeplfaeeqpeaekpva 432
Cdd:PTZ00452  212 I---KERLCYT-----ALDPQDEKRIYKESNSQ----DSPYKLPDGNILT------------------------------ 249
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 433 avqpvfnlaeyhqlfLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLKARVQ 512
Cdd:PTZ00452  250 ---------------IKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLS 314
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099366621 513 KELLEMRPFQSSFQVHLASSPILDAWHGArDWAVEHMTREEGWITRKDYEEKGGEYLKEHC 573
Cdd:PTZ00452  315 NELTNLVPSQLKIQVAAPPDRRFSAWIGG-SIQCTLSTQQPQWIKRQEYDEQGPSIVHRKC 374
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
31-267 3.60e-13

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 71.69  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  31 PVpLVIDNGSFQTRAGWAA-ADPSVPAEPLLRFRSLAARSRGARGGAGAETQVGNDlGSPEPLRWLLRSPFDRNVPVQLE 109
Cdd:PTZ00280    5 PV-VVIDNGTGYTKMGYAGnTEPTYIIPTLIADNSKQSRRRSKKGFEDLDFYIGDE-ALAASKSYTLTYPMKHGIVEDWD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 110 LQELLFDH-VFQRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVDSLYSFYHN--RRQNWPC--- 183
Cdd:PTZ00280   83 LMEKFWEQcIFKYLRCEPE---EHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtSKKAKELggt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 184 -SGLVISSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKYPGHFAAITLSRMEEILHEHSYIAEDYTEEL 262
Cdd:PTZ00280  160 lTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEF 239

                  ....*
gi 2099366621 263 QKWRS 267
Cdd:PTZ00280  240 EKYDS 244
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
404-565 1.33e-11

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: 66.26  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 404 EQSLEDVESINEFEPLFAEEQPEAEKPVAAVQPV-FNLAEYHQLFLGTERIRAPEIIFQPSLIGEDQTGIAETMQYVLER 482
Cdd:cd10209   182 KLDRSIVERLKEAVAWSADDEEAYEKKVLTCSPEtYTLPDGRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVST 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 483 YSKEQQALLVQNVFLTGGNAMYPGLKARVQKELL-----EMRPFqssfqvhLASSPildawhgarDWAVEHMTREEGW-- 555
Cdd:cd10209   262 SPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRllsspSSRPA-------LVKPP---------EYMPENTLRYSAWig 325
                         170       180
                  ....*....|....*....|....
gi 2099366621 556 --------------ITRKDYEEKG 565
Cdd:cd10209   326 gailakvvfpqnqhVTKADYDETG 349
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
34-217 1.39e-10

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: 63.74  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAAD------PSVPAEpllrFRSLAARSRGARGGAGAETQV---GNDLGSPEPLrwLLRSPFDRNV 104
Cdd:cd13395     7 LVLDIGSYSTRAGYAGEDtpkavfPSVVGV----VTDDDDAEDYVGGSGEKKRKYyigTNSIGVPRPN--MEVISPLKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 105 PVQ-LELQELLFDHVF-QRLGVASQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYQVPkvsygvdSLY--------SFY 174
Cdd:cd13395    81 LIEdWDAFEKLWDHALkNRLRVDPS---EHPLLLTEPSWNTRANREKLTELMFEKYNVP-------AFFlaknavlsAFA 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2099366621 175 HNRRqnwpcSGLVISSGYQCTHILPVLEGRLDAKNCKRINLGG 217
Cdd:cd13395   151 NGRS-----TALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGG 188
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
131-271 3.78e-09

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: 59.12  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 131 DHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSYGVD---SLYSFYHNRRQNWPC-SGLVISSGYQCTHILPVLEGRLD 206
Cdd:cd10221   101 DHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQavlALAASWTSRKVGERTlTGTVIDSGDGVTHVIPVAEGYVI 180
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099366621 207 AKNCKRINLGGCQAAVYLQRLLQLKYPGHFAAITLSRMEEILHEHSYIAEDYTEELQKW-RSPEYY 271
Cdd:cd10221   181 GSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYdSDPAKY 246
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
405-565 1.86e-08

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: 56.40  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 405 QSLEDVESINEfEPLFAEEQPEAEKpVAAVQPVFNLAEYHQLFLGTERIRAPEIIFQPSLIGEDQTG----IAETMQYVL 480
Cdd:cd13396   169 PSLYTVRTIKE-KLCYVAEDYEAEL-AKDTQASCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGlhqaVALCMDHCA 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 481 ERYSKEQQALLvQNVFLTGGNAMYPGLKARVQKELLEMRPFQSSFQVHLASSPI--LDAWHGARdwAVEHMTR-EEGW-I 556
Cdd:cd13396   247 LVHSQGDDGWF-KTIVLSGGSACLPGLSERLERELRKLLPKSLSEGIRIIPPPLgpDSAWQGAK--LISNLSNfPDGWcI 323

                  ....*....
gi 2099366621 557 TRKDYEEKG 565
Cdd:cd13396   324 TKKQFRNKP 332
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
34-233 7.13e-08

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: 54.62  E-value: 7.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAADPSVPaePLLRFRSLAarsrgarggagaetqvgndlgspePLRWllrsPFDRNVPVQLELQEL 113
Cdd:cd10208     3 LVIDPGSQTTRAGLGLGELLTP--PTIEIPTRV------------------------EIIW----PIQDGRVVDWDALEA 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 114 LFDHVFQRLGVASQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYQVPKVSY---GVDSLYSFyhnrrqNWPcSGLVISS 190
Cdd:cd10208    53 LWRHILFSLLSIPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAIleaPLAALYAA------GAT-SGIVVDI 125
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2099366621 191 GYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKYP 233
Cdd:cd10208   126 GHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEP 168
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
34-257 2.48e-07

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: 53.16  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621  34 LVIDNGSFQTRAGWAAAD--PSVpAEPllrfrslAARSRGARGGAGAETQVGNDLGSPePLRWLLRSpFDrnvpvqlELQ 111
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDrePSV-VEP-------TRVTPAVEDGEESDTVVEGNTVSP-IRRGRIED-WD-------ALE 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 112 ELLFDHVFQRLG--VASQGCVdhpiVLTEAVCNPLYSRQMMSELLFECYQVP---KVSYGVDSLYSFYHnrrqnwpCSGL 186
Cdd:cd10209    64 ALLRYVFYTGLGweEGNEGQV----LIAEPLLTSKAERERLTQLMFETFNVSglyASEQAVLSLYAVGR-------ISGC 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099366621 187 VISSGYQCTHILPVLEGRLDAKNCKRINLGGCQAAVYLQRLLQLKYPghFAAITLSRMEEILHEHSYIAED 257
Cdd:cd10209   133 VVDVGHGKIDIAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEAVAWSADD 201
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
105-264 1.10e-06

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: 51.01  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 105 PVQLELQELLFDhVFQRLGVASQGcvdHPIVLTEAVCN------PLYSRQMMSELLFECY---QVPKVSYGVDSLYSFYH 175
Cdd:cd13396    36 PMYARLCHFVFT-IMTRMQVKPSR---QPVVVSLPLCHsddtesAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 176 NRRqnwpCSGLVISSGYQCTHILPVLEGR-LDAKNCKRINLGGCQAAVYLQRLLQ---LKYPGHFAAITLSrmEEIlheh 251
Cdd:cd13396   112 ANR----TSGIVVNIGFRVTTIVPVYRGRvMHDIGVEVVGQGALRLTGFLKELMQqngIRFPSLYTVRTIK--EKL---- 181
                         170
                  ....*....|...
gi 2099366621 252 SYIAEDYTEELQK 264
Cdd:cd13396   182 CYVAEDYEAELAK 194
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
134-262 8.27e-06

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: 48.40  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 134 IVLTEAVCNPLYSRQMMSELLFECYQVPKVSY---GVDSLYSFyhnRRQnwpcSGLVISSGYQCTHILPVLEGRLDAKNC 210
Cdd:cd10207    75 VVVVESVLCPTPFRETLAKVLFKHFEVPSVLFapsHLLSLLTL---GIR----TALVVDCGYRETRVLPVYEGVPLLSAW 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2099366621 211 KRINLGGcqAAV--YLQRLLqLKYPGHFAAItlSRMEEILHEHSYIAEDYTEEL 262
Cdd:cd10207   148 QSTPLGG--KALhkRLKKLL-LEHATVVTGD--NKGQLLSSVDSLLSEEVLEDI 196
COG5277 COG5277
Actin-related protein [Cytoskeleton];
451-563 8.29e-04

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 42.08  E-value: 8.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 451 ERIRAPEIIFQPSLIG------------EDQT----------GIAETMQYVLERYSKEQQALLVQNVFLTGGNAMY---P 505
Cdd:COG5277   279 ERFLIGEILFNPNHEGfesyiqqgrlriEDAVigdvvlygemGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpP 358
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099366621 506 GLK-------ARVQKELLEMRPfQSSFQVHLASSPILDAWHGARDWAVE-HMTREEGWITRKDYEE 563
Cdd:COG5277   359 GLEdvavdsvTRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYAlPFSVKWSWITKEGWYF 423
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
457-562 1.67e-03

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: 41.24  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 457 EIIFQPSLIGED---QTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLKARVQKELLEMRPFQ--SSFQVHLAS 531
Cdd:cd10212   309 EYLFKPQLISDKfspEDGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYklTTFANQVMM 388
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2099366621 532 SPILDAWHGARDWAVEHMTREEGWITRKDYE 562
Cdd:cd10212   389 DRKIQGWLGALTMANLPSWSLGKWYSKEDYE 419
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
401-515 4.59e-03

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: 39.60  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099366621 401 LSSEQSLEDVESINEFEPLFaeEQPEAEKPVAAVQPV---FNLAEYHQLFLGTERIRAPEIIFQPSLIGEDqTGIAETMQ 477
Cdd:cd10208   163 LKSDEPELKSQAESGEEATL--DLAEALKKSPICEVLsdgADLASGTEITVGKERFRACEPLFKPSSLRVD-LLIAAIAG 239
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2099366621 478 YVLERYSKE--QQALLVQNVFLTGGNAMYPGLKARVQKEL 515
Cdd:cd10208   240 ALVLNASDEpdKRPALWENIIIVGGGSRIRGLKEALLSEL 279
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
449-515 4.95e-03

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: 39.47  E-value: 4.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099366621 449 GTERIRAPEIIFQPSLIGED-QTGIAETMQYVLERYSKEQQALLVQNVFLTGGNAMYPGLKARVQKEL 515
Cdd:cd10221   266 GYERFLAPEIFFNPEIASSDfTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMFKDFGRRLQRDV 333
 
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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