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Conserved domains on  [gi|2070675846|ref|NP_001382533|]
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actin-related protein 5 [Rattus norvegicus]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
32-570 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: 546.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWACpgpdpGPEPRLQFRAVCARGRGGARGGLGPQVGNALGSLEPLRWMLRSPFDRNVPVNLELQEL 111
Cdd:cd10211     1 PIVIDNGSYQCRAGWAG-----DKEPRLVFRNLVAKPRDRKKGITVTLVGNDILNDEAVRSHLRSPFDRNVVTNFDLQEQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 112 LLDYSFQHLGVSSQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYHNMPKNALSSGLVISSGYQ 191
Cdd:cd10211    76 ILDYIFSHLGINSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQGDPSDGLVISSGYS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 192 CTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYPGHLAAITLSRMEEILQEHSYIAEDYAAELQKWRCPDYYEN 271
Cdd:cd10211   156 TTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYEE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 272 NVHKMQLPFsskllgstltaeekqerrqqqlrrlqelnarrreeklqldqerlerllyvqelledgqmdqfhkalielnm 351
Cdd:cd10211   236 NVRKIQLPF----------------------------------------------------------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 352 dspeelqsyiqkltlaveqakqkilqaeanlevdvvdskpetpdleplepsledvenindfeplfseetpevekpqvttt 431
Cdd:cd10211       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 432 vqpvfnlaayhqlfvgterirapeiifqpsligeeqaGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEK 511
Cdd:cd10211   245 -------------------------------------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEK 287
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2070675846 512 ELLEMRPFQSSFQVQLASNPVLDAWYGARDWALDHlEDSGAWVTRKDYEEKGGEYLKEH 570
Cdd:cd10211   288 ELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDS-TFEKVWITKQEYEEKGGEYLKEH 345
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
339-560 6.22e-06

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 cd10212:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 424  Bit Score: 48.95  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 339 MDQFHKALIELNMDSPEELQSYIQKLTLAVEQAKQKILQAEANLEVDVVDSKPETPdleplepsLEDVENINdFEPLfse 418
Cdd:cd10212   226 IQQFKSTMLQVSEKDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNP--------LVQKKNFL-FKPL--- 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 419 etpeveKPQVTTTVQPVFNLAAYhqlfvgterirapeiIFQPSLIGEE---QAGIAETLHYVLDRYPKAVQDTLVQNVFL 495
Cdd:cd10212   294 ------NKTLTLDLKECYQFAEY---------------LFKPQLISDKfspEDGLGPLMAKSVKKAPEQVYSLLLTNVII 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846 496 TGGNVMYPGMKARVEKELLEMRPFQ--SSFQVQLASNPVLDAWYGARDWALDHLEDSGAWVTRKDYE 560
Cdd:cd10212   353 TGSTSLIEGMEQRIIKELSIRFPQYklTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYE 419
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
32-570 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: 546.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWACpgpdpGPEPRLQFRAVCARGRGGARGGLGPQVGNALGSLEPLRWMLRSPFDRNVPVNLELQEL 111
Cdd:cd10211     1 PIVIDNGSYQCRAGWAG-----DKEPRLVFRNLVAKPRDRKKGITVTLVGNDILNDEAVRSHLRSPFDRNVVTNFDLQEQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 112 LLDYSFQHLGVSSQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYHNMPKNALSSGLVISSGYQ 191
Cdd:cd10211    76 ILDYIFSHLGINSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQGDPSDGLVISSGYS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 192 CTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYPGHLAAITLSRMEEILQEHSYIAEDYAAELQKWRCPDYYEN 271
Cdd:cd10211   156 TTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYEE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 272 NVHKMQLPFsskllgstltaeekqerrqqqlrrlqelnarrreeklqldqerlerllyvqelledgqmdqfhkalielnm 351
Cdd:cd10211   236 NVRKIQLPF----------------------------------------------------------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 352 dspeelqsyiqkltlaveqakqkilqaeanlevdvvdskpetpdleplepsledvenindfeplfseetpevekpqvttt 431
Cdd:cd10211       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 432 vqpvfnlaayhqlfvgterirapeiifqpsligeeqaGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEK 511
Cdd:cd10211   245 -------------------------------------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEK 287
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2070675846 512 ELLEMRPFQSSFQVQLASNPVLDAWYGARDWALDHlEDSGAWVTRKDYEEKGGEYLKEH 570
Cdd:cd10211   288 ELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDS-TFEKVWITKQEYEEKGGEYLKEH 345
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
32-563 1.93e-44

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 162.43  E-value: 1.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846   32 PLVLDNGSFQARAGWAcpGPDpgpEPRLQFRAVCARGRGGARGGLGPQ---VGNALGSLEPLrWMLRSPFDRNVPVNLEL 108
Cdd:smart00268   3 AIVIDNGSGTIKAGFA--GED---FPQVVFPSIVGRPKDGKGMVGDAKdifVGDEAQEKRGG-LELKYPIENGIVENWDD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  109 QELLLDYSFQ-HLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYHNMpknaLSSGLVIS 187
Cdd:smart00268  77 MEKIWDYTFFnELRVEPE---EHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASG----RTTGLVID 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  188 SGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLqlkypghlaaitlsrmEEILQEHSYIAEDYAAelqkwrcpd 267
Cdd:smart00268 150 SGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELL----------------SERGYQFNSSAEFEIV--------- 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  268 yyennvhkmqlpfsskllgstltaeekqerrqqqlrrlqelnarrREEKlqldqerlERLLYVQElledgqmdqfhkali 347
Cdd:smart00268 205 ---------------------------------------------REIK--------EKLCYVAE--------------- 216
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  348 elnmDSPEELQSYiqkltlaveqakqkilqaeanlevdvvdskpetpdlEPLEPSLEDVENindfeplfseetpevekpq 427
Cdd:smart00268 217 ----DFEKEMKLA------------------------------------RESSESSKLEKT------------------- 237
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  428 vtttvqpvFNLAAYHQLFVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKA 507
Cdd:smart00268 238 --------YELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGE 309
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846  508 RVEKELLEMRPFQSSFQVQLASNPVLDAWYGARDWA-LDHLEDSgaWVTRKDYEEKG 563
Cdd:smart00268 310 RLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILAsLSTFEDM--WITKKEYEESG 364
Actin pfam00022
Actin;
32-563 1.03e-29

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 121.64  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWAcpGPDPgpePRLQFRAVCARGRGGARGGLGP-QVGNalGSLEPLRWM-LRSPFDRNVPVNLELQ 109
Cdd:pfam00022   3 ALVIDNGSHTTRAGFA--GEDA---PKAVIPSCVGKPRGTKVEAANKyYVGD--EALTYRPGMeVRSPVEDGIVVDWDAM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 110 ELLLDYSF-QHLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSGLVISS 188
Cdd:pfam00022  76 EEIWEHVLkEELQVDPE---EHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAF----ASGRTTGLVVDS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 189 GYQCTHILPVLEGRLDAKNCKRINLGGsqaagylqrllqlkypghlAAITlsrmeeilqehsyiaeDYAAELqkwrcpdy 268
Cdd:pfam00022 149 GAGVTSVVPVHDGYVLQKAIRRSDLGG-------------------DFLT----------------DYLREL-------- 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 269 yennvhkmqlpFSSKLLGSTLTAEEKQERRQQQLRRLQELNARRREEKLQLDQERlerllyvqELLEDgqmdqfhkalie 348
Cdd:pfam00022 186 -----------LRSRNIEITPRYLIKSKKPGDPAPAVTKRELPDTTYSYKTYQER--------RVLEE------------ 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 349 lnmdspeelqsyiqkltlaveqAKqkilqaEANLEVdvvdskPETPdleplepsledvenindfeplFSEETPEVEKPQV 428
Cdd:pfam00022 235 ----------------------IK------ESVCYV------SDDP---------------------FGDETTSSSIPTR 259
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 429 tttvqpVFNLAAYHQLFVGTERIRAPEIIFQPSLIGEEQA--------GIAETLHYVLDRYPKAVQDTLVQNVFLTGGNV 500
Cdd:pfam00022 260 ------VYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIVVTGGNS 333
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070675846 501 MYPGMKARVEKELleMRPFQSSFQVQLASNPVLD-----AWYGARDWA-LDHLEDSgaWVTRKDYEEKG 563
Cdd:pfam00022 334 LFPGFTERLEKEL--AQLAPPGVKVKIIAPGNTVerrysAWIGGSILAsLGTFQQM--WVSKQEYEEHG 398
PTZ00004 PTZ00004
actin-2; Provisional
33-563 1.22e-21

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 97.15  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  33 LVLDNGSFQARAGWAcpGPDpgpEPRLQFRAVCARGRGGARGGLGPQ----VG----NALGSLEplrwmLRSPFDRNVPV 104
Cdd:PTZ00004    9 AVVDNGSGMVKAGFA--GDD---APRCVFPSIVGRPKNPGIMVGMEEkdcyVGdeaqDKRGILT-----LKYPIEHGIVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 105 NLELQELLLDYSF-QHLGVSSqgcVDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSG 183
Cdd:PTZ00004   79 NWDDMEKIWHHTFyNELRVAP---EEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLY----ASGRTTG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 184 LVISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLqlkyPGHLAAITLSRMEEIL----QEHSYIAEDYAAE 259
Cdd:PTZ00004  152 IVLDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKIL----HERGTTFTTTAEKEIVrdikEKLCYIALDFDEE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 260 lqkwrcpdyyennvhkmqlpfsskllgstltaeekqerrqqqlrrlqelnarrreeklqldqerlerllyvqelledgqm 339
Cdd:PTZ00004      --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 340 dqfhkalielnMDSPEElqsyiqkltlaveqakqkilqaeanlEVDVVDSKPETPDleplepsledvENIndfeplfsee 419
Cdd:PTZ00004  228 -----------MGNSAG--------------------------SSDKYEESYELPD-----------GTI---------- 249
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 420 tpevekpqvtttvqpvfnlaayhqLFVGTERIRAPEIIFQPSLIGEEQA-GIAETLHYVLDRYPKAVQDTLVQNVFLTGG 498
Cdd:PTZ00004  250 ------------------------ITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGG 305
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070675846 499 NVMYPGMKARVEKELLEMRPFQSSFQVQLASNPVLDAWYGARDWA-LDHLEDsgAWVTRKDYEEKG 563
Cdd:PTZ00004  306 TTMYRGLPERLTKELTTLAPSTMKIKVVAPPERKYSVWIGGSILSsLPTFQQ--MWVTKEEYDESG 369
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
339-560 6.22e-06

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: 48.95  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 339 MDQFHKALIELNMDSPEELQSYIQKLTLAVEQAKQKILQAEANLEVDVVDSKPETPdleplepsLEDVENINdFEPLfse 418
Cdd:cd10212   226 IQQFKSTMLQVSEKDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNP--------LVQKKNFL-FKPL--- 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 419 etpeveKPQVTTTVQPVFNLAAYhqlfvgterirapeiIFQPSLIGEE---QAGIAETLHYVLDRYPKAVQDTLVQNVFL 495
Cdd:cd10212   294 ------NKTLTLDLKECYQFAEY---------------LFKPQLISDKfspEDGLGPLMAKSVKKAPEQVYSLLLTNVII 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846 496 TGGNVMYPGMKARVEKELLEMRPFQ--SSFQVQLASNPVLDAWYGARDWALDHLEDSGAWVTRKDYE 560
Cdd:cd10212   353 TGSTSLIEGMEQRIIKELSIRFPQYklTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYE 419
COG5277 COG5277
Actin-related protein [Cytoskeleton];
449-561 6.36e-05

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 45.55  E-value: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 449 ERIRAPEIIFQPSLIGEE----------------------QAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMY---P 503
Cdd:COG5277   279 ERFLIGEILFNPNHEGFEsyiqqgrlriedavigdvvlygEMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpP 358
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846 504 GMK-------ARVEKELLEMRPfQSSFQVQLASNPVLDAWYGARDWALDhLEDSGAW--VTRKDYEE 561
Cdd:COG5277   359 GLEdvavdsvTRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYA-LPFSVKWswITKEGWYF 423
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
32-570 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: 546.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWACpgpdpGPEPRLQFRAVCARGRGGARGGLGPQVGNALGSLEPLRWMLRSPFDRNVPVNLELQEL 111
Cdd:cd10211     1 PIVIDNGSYQCRAGWAG-----DKEPRLVFRNLVAKPRDRKKGITVTLVGNDILNDEAVRSHLRSPFDRNVVTNFDLQEQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 112 LLDYSFQHLGVSSQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYHNMPKNALSSGLVISSGYQ 191
Cdd:cd10211    76 ILDYIFSHLGINSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQGDPSDGLVISSGYS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 192 CTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYPGHLAAITLSRMEEILQEHSYIAEDYAAELQKWRCPDYYEN 271
Cdd:cd10211   156 TTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYEE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 272 NVHKMQLPFsskllgstltaeekqerrqqqlrrlqelnarrreeklqldqerlerllyvqelledgqmdqfhkalielnm 351
Cdd:cd10211   236 NVRKIQLPF----------------------------------------------------------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 352 dspeelqsyiqkltlaveqakqkilqaeanlevdvvdskpetpdleplepsledvenindfeplfseetpevekpqvttt 431
Cdd:cd10211       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 432 vqpvfnlaayhqlfvgterirapeiifqpsligeeqaGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEK 511
Cdd:cd10211   245 -------------------------------------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEK 287
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2070675846 512 ELLEMRPFQSSFQVQLASNPVLDAWYGARDWALDHlEDSGAWVTRKDYEEKGGEYLKEH 570
Cdd:cd10211   288 ELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDS-TFEKVWITKQEYEEKGGEYLKEH 345
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
32-563 1.93e-44

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 162.43  E-value: 1.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846   32 PLVLDNGSFQARAGWAcpGPDpgpEPRLQFRAVCARGRGGARGGLGPQ---VGNALGSLEPLrWMLRSPFDRNVPVNLEL 108
Cdd:smart00268   3 AIVIDNGSGTIKAGFA--GED---FPQVVFPSIVGRPKDGKGMVGDAKdifVGDEAQEKRGG-LELKYPIENGIVENWDD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  109 QELLLDYSFQ-HLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYHNMpknaLSSGLVIS 187
Cdd:smart00268  77 MEKIWDYTFFnELRVEPE---EHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASG----RTTGLVID 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  188 SGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLqlkypghlaaitlsrmEEILQEHSYIAEDYAAelqkwrcpd 267
Cdd:smart00268 150 SGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELL----------------SERGYQFNSSAEFEIV--------- 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  268 yyennvhkmqlpfsskllgstltaeekqerrqqqlrrlqelnarrREEKlqldqerlERLLYVQElledgqmdqfhkali 347
Cdd:smart00268 205 ---------------------------------------------REIK--------EKLCYVAE--------------- 216
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  348 elnmDSPEELQSYiqkltlaveqakqkilqaeanlevdvvdskpetpdlEPLEPSLEDVENindfeplfseetpevekpq 427
Cdd:smart00268 217 ----DFEKEMKLA------------------------------------RESSESSKLEKT------------------- 237
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  428 vtttvqpvFNLAAYHQLFVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKA 507
Cdd:smart00268 238 --------YELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGE 309
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846  508 RVEKELLEMRPFQSSFQVQLASNPVLDAWYGARDWA-LDHLEDSgaWVTRKDYEEKG 563
Cdd:smart00268 310 RLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILAsLSTFEDM--WITKKEYEESG 364
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
33-563 1.93e-43

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: 160.02  E-value: 1.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  33 LVLDNGSFQARAGWACPGPdpgpePRLQFRAVCARGRGGARGGLGPQV--GNALGSLeplrwMLRSPFDRNVPVNLELQE 110
Cdd:cd10210     2 LVLDNGAYTIKAGFASDDP-----PRVIPNCIAKPKSERRRLFGDDQLdeCKDLSGL-----FYRRPFERGYLVNWDLQR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 111 LLLDYSFQHLGVSsQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYripkvayGIDSLF-------SFYHNMPKNALSSG 183
Cdd:cd10210    72 QIWDHLFGKLLLN-VDPSDTALVLTEPPFNPPSIQEAMDEIVFEEY-------GFQSLYrttaaalSAFAYLADSEQSSS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 184 ------LVISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYpghlaaITLSR----MEEILQEHSYIA 253
Cdd:cd10210   144 sssqccLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQ------LNVMDetylVNQIKEDLCFVS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 254 EDYAAELQKwrcpdyyennvhkmqlpfsskllgstltaeekqerrqqqlrrlqelnARRREEKLQLDQErlerllYVqel 333
Cdd:cd10210   218 TDFYEDLEI-----------------------------------------------AKKKGKENTIRRD------YV--- 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 334 LEDGQmDQFHKALIELNMDSPEELQSYIQKLTLaveqakqkilqaeanlevdvvdskpetpdleplepsledvenindfe 413
Cdd:cd10210   242 LPDYT-TSKRGYVRDPEEPNRGKLKEDEQVLRL----------------------------------------------- 273
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 414 plfseetpevekpqvtttvqpvfnlaayhqlfvGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNV 493
Cdd:cd10210   274 ---------------------------------NNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYANI 320
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 494 FLTGGNVMYPGMKARVEKELLEMRPFQSSFQVQLASNPVLDAWYGARDWALDHlEDSGAWVTRKDYEEKG 563
Cdd:cd10210   321 VLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSP-EFEELAVTRAEYEEHG 389
Actin pfam00022
Actin;
32-563 1.03e-29

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 121.64  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWAcpGPDPgpePRLQFRAVCARGRGGARGGLGP-QVGNalGSLEPLRWM-LRSPFDRNVPVNLELQ 109
Cdd:pfam00022   3 ALVIDNGSHTTRAGFA--GEDA---PKAVIPSCVGKPRGTKVEAANKyYVGD--EALTYRPGMeVRSPVEDGIVVDWDAM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 110 ELLLDYSF-QHLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSGLVISS 188
Cdd:pfam00022  76 EEIWEHVLkEELQVDPE---EHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAF----ASGRTTGLVVDS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 189 GYQCTHILPVLEGRLDAKNCKRINLGGsqaagylqrllqlkypghlAAITlsrmeeilqehsyiaeDYAAELqkwrcpdy 268
Cdd:pfam00022 149 GAGVTSVVPVHDGYVLQKAIRRSDLGG-------------------DFLT----------------DYLREL-------- 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 269 yennvhkmqlpFSSKLLGSTLTAEEKQERRQQQLRRLQELNARRREEKLQLDQERlerllyvqELLEDgqmdqfhkalie 348
Cdd:pfam00022 186 -----------LRSRNIEITPRYLIKSKKPGDPAPAVTKRELPDTTYSYKTYQER--------RVLEE------------ 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 349 lnmdspeelqsyiqkltlaveqAKqkilqaEANLEVdvvdskPETPdleplepsledvenindfeplFSEETPEVEKPQV 428
Cdd:pfam00022 235 ----------------------IK------ESVCYV------SDDP---------------------FGDETTSSSIPTR 259
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 429 tttvqpVFNLAAYHQLFVGTERIRAPEIIFQPSLIGEEQA--------GIAETLHYVLDRYPKAVQDTLVQNVFLTGGNV 500
Cdd:pfam00022 260 ------VYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIVVTGGNS 333
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070675846 501 MYPGMKARVEKELleMRPFQSSFQVQLASNPVLD-----AWYGARDWA-LDHLEDSgaWVTRKDYEEKG 563
Cdd:pfam00022 334 LFPGFTERLEKEL--AQLAPPGVKVKIIAPGNTVerrysAWIGGSILAsLGTFQQM--WVSKQEYEEHG 398
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
33-229 5.06e-29

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


Pssm-ID: 466810 [Multi-domain]  Cd Length: 258  Bit Score: 116.05  E-value: 5.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  33 LVLDNGSFQARAGWAcpGPDpgpEPRLQFravcargrggargglgpqvgnalgsleplrwmlrsPFDRnvpvnlelQELL 112
Cdd:cd10169     1 IVIDNGSGTIKAGFA--GED---APRLIF-----------------------------------PWDD--------MEKI 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 113 LDYSFQHLGVSSQgcVDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYHNmpknALSSGLVISSGYQC 192
Cdd:cd10169    33 WEHVFYNLLRVDP--EEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYAS----GRTTGLVVDSGEGV 106
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2070675846 193 THILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLK 229
Cdd:cd10169   107 THIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREK 143
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
32-563 6.29e-28

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: 115.36  E-value: 6.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWAcpGPDpgpEPRLQFRAVCARGRGGARGGLGPQ----VGN-ALGSLEPLRwmLRSPFDRNVPVNL 106
Cdd:cd13397     2 AVVIDNGSGLIKAGFA--GED---LPRAVFPSVVGRPKYKAVMLGAGQkevyVGDeAQEKRGVLT--LSYPIEHGIVTNW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 107 ELQELLLDYSFQH-LGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSGLV 185
Cdd:cd13397    75 DDMEKIWHHTFENeLRVKPE---EHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLY----SSGRTTGLV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 186 ISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKypGHLAAITLSR--MEEILQEHSYIAEDYAAELQKW 263
Cdd:cd13397   148 LDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKER--GHSFTTTAEReiVRDIKEKLCYVALDYEEELKKK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 264 RcpdyyENNVHKMQLPfsskllgstltaeekqerrqqqlrrlqelnarrreeklqldqerlerllyvqelleDGQmdqfh 343
Cdd:cd13397   226 S-----EELEKEYTLP--------------------------------------------------------DGQ----- 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 344 kaLIELnmdspeelqsyiqkltlaveqakqkilqaeanlevdvvdskpetpdleplepsledvenindfeplfseetpev 423
Cdd:cd13397   240 --VIKI-------------------------------------------------------------------------- 243
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 424 ekpqvtttvqpvfnlaayhqlfvGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYP 503
Cdd:cd13397   244 -----------------------GSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFP 300
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846 504 GMKARVEKELLEMRPfqSSFQVQLASNPvlDAWYGArdW-------ALDHLEDsgAWVTRKDYEEKG 563
Cdd:cd13397   301 GLPERLQKELEALAP--SSTKVKVIAPP--ERKYSV--WiggsilaSLSTFKS--MWITRAEYDEFG 359
PTZ00004 PTZ00004
actin-2; Provisional
33-563 1.22e-21

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 97.15  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  33 LVLDNGSFQARAGWAcpGPDpgpEPRLQFRAVCARGRGGARGGLGPQ----VG----NALGSLEplrwmLRSPFDRNVPV 104
Cdd:PTZ00004    9 AVVDNGSGMVKAGFA--GDD---APRCVFPSIVGRPKNPGIMVGMEEkdcyVGdeaqDKRGILT-----LKYPIEHGIVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 105 NLELQELLLDYSF-QHLGVSSqgcVDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSG 183
Cdd:PTZ00004   79 NWDDMEKIWHHTFyNELRVAP---EEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLY----ASGRTTG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 184 LVISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLqlkyPGHLAAITLSRMEEIL----QEHSYIAEDYAAE 259
Cdd:PTZ00004  152 IVLDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKIL----HERGTTFTTTAEKEIVrdikEKLCYIALDFDEE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 260 lqkwrcpdyyennvhkmqlpfsskllgstltaeekqerrqqqlrrlqelnarrreeklqldqerlerllyvqelledgqm 339
Cdd:PTZ00004      --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 340 dqfhkalielnMDSPEElqsyiqkltlaveqakqkilqaeanlEVDVVDSKPETPDleplepsledvENIndfeplfsee 419
Cdd:PTZ00004  228 -----------MGNSAG--------------------------SSDKYEESYELPD-----------GTI---------- 249
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 420 tpevekpqvtttvqpvfnlaayhqLFVGTERIRAPEIIFQPSLIGEEQA-GIAETLHYVLDRYPKAVQDTLVQNVFLTGG 498
Cdd:PTZ00004  250 ------------------------ITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGG 305
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070675846 499 NVMYPGMKARVEKELLEMRPFQSSFQVQLASNPVLDAWYGARDWA-LDHLEDsgAWVTRKDYEEKG 563
Cdd:PTZ00004  306 TTMYRGLPERLTKELTTLAPSTMKIKVVAPPERKYSVWIGGSILSsLPTFQQ--MWVTKEEYDESG 369
PTZ00281 PTZ00281
actin; Provisional
33-571 3.77e-20

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 92.84  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  33 LVLDNGSFQARAGWAcpGPDPgpePRLQFRAVCARGRGGARGGLGPQVGNALGSLEPLR---WMLRSPFDRNVPVNLELQ 109
Cdd:PTZ00281    9 LVIDNGSGMCKAGFA--GDDA---PRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKrgiLTLKYPIEHGIVTNWDDM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 110 ELLLDYSF-QHLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSGLVISS 188
Cdd:PTZ00281   84 EKIWHHTFyNELRVAPE---EHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLY----ASGRTTGIVMDS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 189 GYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKypGHLAAITLSR--MEEILQEHSYIAEDYAAELQKwrcp 266
Cdd:PTZ00281  157 GDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTER--GYSFTTTAEReiVRDIKEKLAYVALDFEAEMQT---- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 267 dyyennvhkmqlpfsskllGSTLTAEEKqerrqqqlrrlqelnarrreeklqldqerlerllyvqelledgqmdqfhkal 346
Cdd:PTZ00281  231 -------------------AASSSALEK---------------------------------------------------- 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 347 ielnmdspeelqSYiqkltlaveqakqkilqaeanlevdvvdskpETPDleplepsledvenindfeplfseetpevekP 426
Cdd:PTZ00281  240 ------------SY-------------------------------ELPD------------------------------G 246
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 427 QVTTtvqpvfnlaayhqlfVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMK 506
Cdd:PTZ00281  247 QVIT---------------IGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIA 311
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070675846 507 ARVEKELLEMRPfqSSFQVQLASNP--VLDAWYGARDWA-LDHLEDsgAWVTRKDYEEKGGEYLKEHC 571
Cdd:PTZ00281  312 DRMNKELTALAP--STMKIKIIAPPerKYSVWIGGSILAsLSTFQQ--MWISKEEYDESGPSIVHRKC 375
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
129-563 9.60e-18

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: 85.11  E-value: 9.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 129 DHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSGLVISSGYQCTHILPVLEGRLDAKNC 208
Cdd:cd10224    95 EHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLY----ASGRTTGIVLDSGDGVSHTVPIYEGYALPHAI 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 209 KRINLGGSQAAGYLQRllqlkypghlaaitlsrmeeILQEHSYiaedyaaelqkwrcpdyyennvhkmqlPFsskllgsT 288
Cdd:cd10224   171 LRLDLAGRDLTDYLMK--------------------ILTERGY---------------------------SF-------T 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 289 LTAEEKQErrqqqlrrlqelnarrREEKlqldqerlERLLYVqelledgqmdqfhkALielnmDSPEELQSYIQKLTLav 368
Cdd:cd10224   197 TTAEREIV----------------RDIK--------EKLCYV--------------AL-----DFEQEMQTAASSSSL-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 369 eqakqkilqaeanlevdvvdskpetpdleplepsledvenindfeplfsEETPEVEKPQVTTtvqpvfnlaayhqlfVGT 448
Cdd:cd10224   232 -------------------------------------------------EKSYELPDGQVIT---------------IGN 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 449 ERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEKELLEMRPfqSSFQVQLA 528
Cdd:cd10224   248 ERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAP--STMKIKIV 325
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 2070675846 529 SNP--VLDAWYGARDWA-LDHLEDsgAWVTRKDYEEKG 563
Cdd:cd10224   326 APPerKYSVWIGGSILAsLSTFQQ--MWISKQEYDESG 361
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
94-568 2.27e-17

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: 84.15  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  94 LRSPFDRNVPV------NLELQELLLDYSFQH-LGVSSQGCvdhPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGID 166
Cdd:cd10220    58 LRSMLEVTYPMengivrNWDDMEHLWDYTFGEkLKIDPREC---KILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQ 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 167 SLFSFYhnmpKNALSSGLVISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLK-YP-GHLAAITLSRmeE 244
Cdd:cd10220   135 AVLTLY----AQGLLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRgYAfNRTADFETVR--E 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 245 ILQEHSYIAEDYAAELQkwrcpdyyennvhkmqlpfsskllgstltaeekqerrqqqlrrlqelnarrreeklqldqerl 324
Cdd:cd10220   209 IKEKLCYVAYDIELEQK--------------------------------------------------------------- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 325 erllyvqelledgqmdqfhkalielnmdspeelqsyiqkltLAVEqakqkilqaeanlevdvvdskpetpdleplepsle 404
Cdd:cd10220   226 -----------------------------------------LALE----------------------------------- 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 405 dvenindfeplfseetpevekpqvTTTVQPVFNLAAYHQLFVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKA 484
Cdd:cd10220   230 ------------------------TTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADID 285
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 485 VQDTLVQNVFLTGGNVMYPGMKARVEKELLEM---------RPFQSSFQVQLASNP-----------VLDawygardwal 544
Cdd:cd10220   286 TRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylervlkgdTERLSKFKIRIEDPPrrkhmvflggaVLA---------- 355
                         490       500
                  ....*....|....*....|....*
gi 2070675846 545 DHLEDSGA-WVTRKDYEEKGGEYLK 568
Cdd:cd10220   356 DIMKDKDEfWITRQEYEEQGVRVLD 380
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
465-563 8.79e-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: 77.53  E-value: 8.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 465 EEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEKELLEMRPFQSSFQVQLASNPVLDAWYGARDWA- 543
Cdd:cd10169   161 EKLCGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKVKVIAPPERKYSAWIGGSILAs 240
                          90       100
                  ....*....|....*....|
gi 2070675846 544 LDHLEDSgaWVTRKDYEEKG 563
Cdd:cd10169   241 LSTFQQM--WITKEEYEEHG 258
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
32-563 1.06e-14

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: 76.04  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWAcpGPDpgpEPRLQFRAVcargrggargglgpqVGNA------LGSLEPLRWM------------ 93
Cdd:cd10216     3 PVVIDNGSGVIKAGFA--GDD---IPKVVFPSY---------------VGRPkhvrvmAGALEGDVFVgpkaeehrgllk 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  94 LRSPFDRNVPVNLELQELLLDYSFQ--HLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSF 171
Cdd:cd10216    63 IRYPMEHGIVTDWNDMERIWQYVYSklQLNTFSE---EHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 172 YhnmpKNALSSGLVISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQrlLQLKYPGHLaAITLSRMEEIlqehsy 251
Cdd:cd10216   140 Y----ASGRTTGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQ--LLLRKSGYN-FHTSAEFEIV------ 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 252 iaedyaaelqkwrcpdyyennvhkmqlpfsskllgstltaeekqerrqqqlrrlqelnarrREEKlqldqerlERLLYVq 331
Cdd:cd10216   207 -------------------------------------------------------------REIK--------EKACYV- 216
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 332 elledgqmdqfhkaliELNMDspeelqsyiqkltlaveqakqkilqaeanlevdvvdskpetpdleplepsledvenind 411
Cdd:cd10216   217 ----------------ALNPQ----------------------------------------------------------- 221
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 412 feplfSEETPEVEKPQVTTtvqpvFNLAAYHQLFVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQ 491
Cdd:cd10216   222 -----KEEKLEEEKTEKAQ-----YTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYS 291
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070675846 492 NVFLTGGNVMYPGMKARVEKELLEMRPFQSSFQVQLASNPVLDAWYGARDWA-LDHLEDsgAWVTRKDYEEKG 563
Cdd:cd10216   292 NIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILAsLSTFKK--MWVSKKEYEEDG 362
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
442-563 4.53e-14

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: 74.00  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 442 HQLFVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEKELLEMRPfqs 521
Cdd:cd10214   241 HLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCP--- 317
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2070675846 522 sfqvqlASNPVLDA--------WYG----ARDWALDHLedsgaWVTRKDYEEKG 563
Cdd:cd10214   318 ------NDNPIVAAsperkysvWTGgsilASLKSFQQL-----WVRRREYEERG 360
PTZ00452 PTZ00452
actin; Provisional
444-571 1.44e-13

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 72.48  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 444 LFVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEKELLEMRPFQSSF 523
Cdd:PTZ00452  248 LTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLKI 327
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2070675846 524 QVQLASNPVLDAWYGARDWALDHLEDSgAWVTRKDYEEKGGEYLKEHC 571
Cdd:PTZ00452  328 QVAAPPDRRFSAWIGGSIQCTLSTQQP-QWIKRQEYDEQGPSIVHRKC 374
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
33-215 8.06e-12

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: 67.59  E-value: 8.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  33 LVLDNGSFQARAGWAcpGPDpgpEPRLQF-----------RAVCARGRGGARGGLGPQVGNALGSlePLRWMLRSPFDRN 101
Cdd:cd13395     7 LVLDIGSYSTRAGYA--GED---TPKAVFpsvvgvvtdddDAEDYVGGSGEKKRKYYIGTNSIGV--PRPNMEVISPLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 102 VPV-NLELQELLLDYSF-QHLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPkvaygidslfSFYhnMPKNA 179
Cdd:cd13395    80 GLIeDWDAFEKLWDHALkNRLRVDPS---EHPLLLTEPSWNTRANREKLTELMFEKYNVP----------AFF--LAKNA 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2070675846 180 -LSS-------GLVISSGYQCTHILPVLEGRLDAKNCKRINLGG 215
Cdd:cd13395   145 vLSAfangrstALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGG 188
PTZ00466 PTZ00466
actin-like protein; Provisional
32-243 1.39e-11

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 66.51  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  32 PLVLDNGSFQARAGWAcpGPDPgpePRLQFRAVCARGRGGARGGLGPQ----VGNalgSLEPLRWMLR--SPFDRNVPVN 105
Cdd:PTZ00466   14 PIIIDNGTGYIKAGFA--GEDV---PNLVFPSYVGRPKYKRVMAGAVEgnifVGN---KAEEYRGLLKvtYPINHGIIEN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 106 LELQELLLDYSFQHLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpKNALSSGLV 185
Cdd:PTZ00466   86 WNDMENIWIHVYNSMKINSE---EHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLY----SCGKTNGTV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2070675846 186 ISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLlqLKYPGHLAAiTLSRME 243
Cdd:PTZ00466  159 LDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYL--LRKNGHLFN-TSAEME 213
PTZ00466 PTZ00466
actin-like protein; Provisional
443-563 1.69e-11

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 66.12  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 443 QLFVGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEKELLEMRPFQSS 522
Cdd:PTZ00466  252 QILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDIT 331
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2070675846 523 FQVQLASNPVLDAWYGARDWA-LDHLEDsgAWVTRKDYEEKG 563
Cdd:PTZ00466  332 IRISAPPERKFSTFIGGSILAsLATFKK--IWISKQEFDEYG 371
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
129-263 2.70e-11

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 65.91  E-value: 2.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 129 DHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFY------HNMPKNALSSGLVISSGYQCTHILPVLEGR 202
Cdd:PTZ00280  102 EHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRaswtskKAKELGGTLTGTVIDSGDGVTHVIPVVDGY 181
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070675846 203 LDAKNCKRINLGGSQAAGYLQRLLQLKYPGHLAAITLSRMEEILQEHSYIAEDYAAELQKW 263
Cdd:PTZ00280  182 VIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKY 242
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
117-262 6.90e-10

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: 61.43  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 117 FQHLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYHNMPKNALS----SGLVISSGYQC 192
Cdd:cd10221    92 FKYLRCEPE---DHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGertlTGTVIDSGDGV 168
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 193 THILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYPGHLAAITLSRMEEILQEHSYIAEDYAAELQK 262
Cdd:cd10221   169 THVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAK 238
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
446-563 1.09e-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: 54.32  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 446 VGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPGMKARVEKELL-----EMRPFq 520
Cdd:cd10209   227 VGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRllsspSSRPA- 305
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2070675846 521 ssfqvqLASNPvldawygarDWALDHLEDSGAW----------------VTRKDYEEKG 563
Cdd:cd10209   306 ------LVKPP---------EYMPENTLRYSAWiggailakvvfpqnqhVTKADYDETG 349
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
33-255 1.15e-06

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: 50.85  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  33 LVLDNGSFQARAGWACPGPDPGP-EPRLQfravcargrggargglGPQVGNALGSLEPLRWMLRSPFDRNVPVNLELQEL 111
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDREPSVvEPTRV----------------TPAVEDGEESDTVVEGNTVSPIRRGRIEDWDALEA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 112 LLDYSF-QHLG--VSSQGCVdhpiVLTEAVCNPLYSRQMMSELLFECYRIPKVAYGIDSLFSFYhnmpknALS--SGLVI 186
Cdd:cd10209    65 LLRYVFyTGLGweEGNEGQV----LIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLY------AVGriSGCVV 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070675846 187 SSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYPghLAAITLSRMEEILQEHSYIAED 255
Cdd:cd10209   135 DVGHGKIDIAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEAVAWSADD 201
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
107-229 2.43e-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: 49.94  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 107 ELQELLLDYSFQHLGVSSQgcvDHPIVLTEAVCNPLYSRQMMSELLFECYRIPKVAY---GIDSLFSFyhnmpknALSSG 183
Cdd:cd10207    53 ALKEFLHELYFKHLLVNPK---DRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFapsHLLSLLTL-------GIRTA 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2070675846 184 LVISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLK 229
Cdd:cd10207   123 LVVDCGYRETRVLPVYEGVPLLSAWQSTPLGGKALHKRLKKLLLEH 168
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
339-560 6.22e-06

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: 48.95  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 339 MDQFHKALIELNMDSPEELQSYIQKLTLAVEQAKQKILQAEANLEVDVVDSKPETPdleplepsLEDVENINdFEPLfse 418
Cdd:cd10212   226 IQQFKSTMLQVSEKDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNP--------LVQKKNFL-FKPL--- 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 419 etpeveKPQVTTTVQPVFNLAAYhqlfvgterirapeiIFQPSLIGEE---QAGIAETLHYVLDRYPKAVQDTLVQNVFL 495
Cdd:cd10212   294 ------NKTLTLDLKECYQFAEY---------------LFKPQLISDKfspEDGLGPLMAKSVKKAPEQVYSLLLTNVII 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846 496 TGGNVMYPGMKARVEKELLEMRPFQ--SSFQVQLASNPVLDAWYGARDWALDHLEDSGAWVTRKDYE 560
Cdd:cd10212   353 TGSTSLIEGMEQRIIKELSIRFPQYklTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYE 419
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
86-231 9.54e-06

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: 48.07  E-value: 9.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846  86 SLEPLRWMLRS------PFDRNVPVNLELQELLLDYSFQHLGVSSQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYRIP 159
Cdd:cd10208    21 LLTPPTIEIPTrveiiwPIQDGRVVDWDALEALWRHILFSLLSIPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVP 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070675846 160 KVAYGIDSLFSFYHNmpkNALSsGLVISSGYQCTHILPVLEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYP 231
Cdd:cd10208   101 AFAILEAPLAALYAA---GATS-GIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEP 168
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
446-563 2.38e-05

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: 46.77  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 446 VGTERIRAPEIIFQPSLIGEEQAGIAETLHYVLDR-YPKAVQ--DTLVQNVFLTGGNVMYPGMKARVEKELLEMRPFQSS 522
Cdd:cd13396   210 LSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHcALVHSQgdDGWFKTIVLSGGSACLPGLSERLERELRKLLPKSLS 289
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2070675846 523 FQVQLASNP--VLDAWYGARdwALDHLED-SGAW-VTRKDYEEKG 563
Cdd:cd13396   290 EGIRIIPPPlgPDSAWQGAK--LISNLSNfPDGWcITKKQFRNKP 332
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
131-262 5.09e-05

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: 45.61  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 131 PIVLTEAVCN------PLYSRQMMSELLFECY---RIPKVAYGIDSLFSFYHNMPknalSSGLVISSGYQCTHILPVLEG 201
Cdd:cd13396    60 PVVVSLPLCHsddtesAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANR----TSGIVVNIGFRVTTIVPVYRG 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070675846 202 R-LDAKNCKRINLGGSQAAGYLQRLLQLKYPGHLAAITLSRMEEILqehSYIAEDYAAELQK 262
Cdd:cd13396   136 RvMHDIGVEVVGQGALRLTGFLKELMQQNGIRFPSLYTVRTIKEKL---CYVAEDYEAELAK 194
COG5277 COG5277
Actin-related protein [Cytoskeleton];
449-561 6.36e-05

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 45.55  E-value: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 449 ERIRAPEIIFQPSLIGEE----------------------QAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMY---P 503
Cdd:COG5277   279 ERFLIGEILFNPNHEGFEsyiqqgrlriedavigdvvlygEMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpP 358
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070675846 504 GMK-------ARVEKELLEMRPfQSSFQVQLASNPVLDAWYGARDWALDhLEDSGAW--VTRKDYEE 561
Cdd:COG5277   359 GLEdvavdsvTRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYA-LPFSVKWswITKEGWYF 423
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
446-563 8.15e-04

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: 42.17  E-value: 8.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070675846 446 VGTERIRAPEIIFQPSLIGEE-QAGIAETLHYVLDRYPKAVQDTLVQNVFLTGGNVMYPG--------MKARVEK----- 511
Cdd:cd10221   265 VGYERFLAPEIFFNPEIASSDfTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMFKDfgrrlqrdVKRIVDArlkas 344
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2070675846 512 -ELLEMRPFQSSFQVQLASNP-----VldaWYGARDWALDHlEDSGAWVTRKDYEEKG 563
Cdd:cd10221   345 eELSGGKLKPKPIDVNVISHPmqryaV---WFGGSMLASTP-EFYTVCHTKAEYEEYG 398
 
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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